3gxe - Revision history

OCA at 15:45, 1 November 2023

OCA — Wed, 01 Nov 2023 15:45:54 GMT

←Older revision		Revision as of 15:45, 1 November 2023
Line 3:		Line 3:
	<StructureSection load='3gxe' size='340' side='right'caption='[[3gxe]], [[Resolution\|resolution]] 2.60Å' scene=''>		<StructureSection load='3gxe' size='340' side='right'caption='[[3gxe]], [[Resolution\|resolution]] 2.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3gxe]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GXE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GXE FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3gxe]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GXE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GXE FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>~~, ~~<scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>~~</td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.6Å</td></tr>
-	<tr id='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non-Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat"><scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene>, <scene name='pdbligand=HZP:(4S)-4-HYDROXY-L-PROLINE'>HZP</scene><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene>, <scene name='pdbligand=HZP:(4S)-4-HYDROXY-L-PROLINE'>HZP</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
-	~~<tr id~~='~~related'><td class~~=~~"sblockLbl"><b>[[Related_structure\|Related~~:~~]]</b></td><td class="sblockDat"><div style='overflow: auto; max~~-~~height: 3em;~~'>~~[[3ejh\|3ejh]]~~</~~div~~>~~</td></tr>~~	+
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FN ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])~~</td></tr>	+
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3gxe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gxe OCA], [https://pdbe.org/3gxe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gxe RCSB], [https://www.ebi.ac.uk/pdbsum/3gxe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gxe ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3gxe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gxe OCA], [https://pdbe.org/3gxe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gxe RCSB], [https://www.ebi.ac.uk/pdbsum/3gxe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gxe ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/FINC_HUMAN FINC_HUMAN]] Defects in FN1 are the cause of glomerulopathy with fibronectin deposits type 2 (GFND2) [MIM:[https://omim.org/entry/601894 601894]]; also known as familial glomerular nephritis with fibronectin deposits or fibronectin glomerulopathy. GFND is a genetically heterogeneous autosomal dominant disorder characterized clinically by proteinuria, microscopic hematuria, and hypertension that leads to end-stage renal failure in the second to fifth decade of life.<ref>PMID:18268355</ref> [[https://www.uniprot.org/uniprot/CO1A1_HUMAN CO1A1_HUMAN]] Defects in COL1A1 are the cause of Caffey disease (CAFFD) [MIM:[https://omim.org/entry/114000 114000]]; also known as infantile cortical hyperostosis. Caffey disease is characterized by an infantile episode of massive subperiosteal new bone formation that typically involves the diaphyses of the long bones, mandible, and clavicles. The involved bones may also appear inflamed, with painful swelling and systemic fever often accompanying the illness. The bone changes usually begin before 5 months of age and resolve before 2 years of age.<ref>PMID:8988177</ref> <ref>PMID:12660034</ref> <ref>PMID:15864348</ref> Defects in COL1A1 are a cause of Ehlers-Danlos syndrome type 1 (EDS1) [MIM:[https://omim.org/entry/130000 130000]]; also known as Ehlers-Danlos syndrome gravis. EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS1 is the severe form of classic Ehlers-Danlos syndrome.<ref>PMID:8988177</ref> <ref>PMID:12660034</ref> <ref>PMID:10739762</ref> <ref>PMID:17211858</ref> Defects in COL1A1 are the cause of Ehlers-Danlos syndrome type 7A (EDS7A) [MIM:[https://omim.org/entry/130060 130060]]; also known as autosomal dominant Ehlers-Danlos syndrome type VII. EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS7A is marked by bilateral congenital hip dislocation, hyperlaxity of the joints, and recurrent partial dislocations.<ref>PMID:8988177</ref> <ref>PMID:12660034</ref> Defects in COL1A1 are a cause of osteogenesis imperfecta type 1 (OI1) [MIM:[https://omim.org/entry/166200 166200]]. A dominantly inherited connective tissue disorder characterized by bone fragility and blue sclerae. Osteogenesis imperfecta type 1 is non-deforming with normal height or mild short stature, and no dentinogenesis imperfecta.<ref>PMID:8988177</ref> <ref>PMID:12660034</ref> <ref>PMID:3244312</ref> <ref>PMID:2794057</ref> <ref>PMID:1718984</ref> <ref>PMID:1634225</ref> <ref>PMID:1737847</ref> <ref>PMID:8223589</ref> <ref>PMID:16705691</ref> <ref>PMID:16786509</ref> <ref>PMID:16638323</ref> <ref>PMID:17875077</ref> <ref>PMID:18670065</ref> Defects in COL1A1 are a cause of osteogenesis imperfecta type 2 (OI2) [MIM:[https://omim.org/entry/166210 166210]]; also known as osteogenesis imperfecta congenita. A connective tissue disorder characterized by bone fragility, with many perinatal fractures, severe bowing of long bones, undermineralization, and death in the perinatal period due to respiratory insufficiency. Defects in COL1A1 are a cause of osteogenesis imperfecta type 3 (OI3) [MIM:[https://omim.org/entry/259420 259420]]. A connective tissue disorder characterized by progressively deforming bones, very short stature, a triangular face, severe scoliosis, grayish sclera, and dentinogenesis imperfecta. Defects in COL1A1 are a cause of osteogenesis imperfecta type 4 (OI4) [MIM:[https://omim.org/entry/166220 166220]]; also known as osteogenesis imperfecta with normal sclerae. A connective tissue disorder characterized by moderately short stature, mild to moderate scoliosis, grayish or white sclera and dentinogenesis imperfecta. Genetic variations in COL1A1 are a cause of susceptibility to osteoporosis (OSTEOP) [MIM:[https://omim.org/entry/166710 166710]]; also known as involutional or senile osteoporosis or postmenopausal osteoporosis. Osteoporosis is characterized by reduced bone mass, disruption of bone microarchitecture without alteration in the composition of bone. Osteoporotic bones are more at risk of fracture.<ref>PMID:8988177</ref> <ref>PMID:12660034</ref> <ref>PMID:8841196</ref> <ref>PMID:9535665</ref> Note=A chromosomal aberration involving COL1A1 is found in dermatofibrosarcoma protuberans. Translocation t(17;22)(q22;q13) with PDGF.<ref>PMID:8988177</ref> <ref>PMID:12660034</ref>	+	[https://www.uniprot.org/uniprot/FINC_HUMAN FINC_HUMAN] Defects in FN1 are the cause of glomerulopathy with fibronectin deposits type 2 (GFND2) [MIM:[https://omim.org/entry/601894 601894]; also known as familial glomerular nephritis with fibronectin deposits or fibronectin glomerulopathy. GFND is a genetically heterogeneous autosomal dominant disorder characterized clinically by proteinuria, microscopic hematuria, and hypertension that leads to end-stage renal failure in the second to fifth decade of life.<ref>PMID:18268355</ref>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/FINC_HUMAN FINC_HUMAN]] Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape.<ref>PMID:8114919</ref> <ref>PMID:11209058</ref> <ref>PMID:15665290</ref> <ref>PMID:19379667</ref> Anastellin binds fibronectin and induces fibril formation. This fibronectin polymer, named superfibronectin, exhibits enhanced adhesive properties. Both anastellin and superfibronectin inhibit tumor growth, angiogenesis and metastasis. Anastellin activates p38 MAPK and inhibits lysophospholipid signaling.<ref>PMID:8114919</ref> <ref>PMID:11209058</ref> <ref>PMID:15665290</ref> <ref>PMID:19379667</ref> ~~[[https://www.uniprot.org/uniprot/CO1A1_HUMAN CO1A1_HUMAN]] Type I collagen is a member of group I collagen (fibrillar forming collagen).~~	+	[https://www.uniprot.org/uniprot/FINC_HUMAN FINC_HUMAN] Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape.<ref>PMID:8114919</ref> <ref>PMID:11209058</ref> <ref>PMID:15665290</ref> <ref>PMID:19379667</ref> Anastellin binds fibronectin and induces fibril formation. This fibronectin polymer, named superfibronectin, exhibits enhanced adhesive properties. Both anastellin and superfibronectin inhibit tumor growth, angiogenesis and metastasis. Anastellin activates p38 MAPK and inhibits lysophospholipid signaling.<ref>PMID:8114919</ref> <ref>PMID:11209058</ref> <ref>PMID:15665290</ref> <ref>PMID:19379667</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Campbell~~, I D~~]]	+	[[Category: Campbell ID]]
-	[[Category: Sladek, B]]	+	[[Category: Sladek B]]
-	[[Category: Vakonakis, I]]	+	[[Category: Vakonakis I]]
-	~~[[Category: Cell adhesion]]~~	+
-	~~[[Category: Protein-peptide complex~~]]	+

OCA at 07:42, 10 November 2021

OCA — Wed, 10 Nov 2021 07:42:42 GMT

←Older revision		Revision as of 07:42, 10 November 2021
Line 1:		Line 1:

	==Complex of a Low Affinity Collagen Site with the Fibronectin 8-9FnI Domain Pair==		==Complex of a Low Affinity Collagen Site with the Fibronectin 8-9FnI Domain Pair==
-	<StructureSection load='3gxe' size='340' side='right' caption='[[3gxe]], [[Resolution\|resolution]] 2.60Å' scene=''>	+	<StructureSection load='3gxe' size='340' side='right'caption='[[3gxe]], [[Resolution\|resolution]] 2.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3gxe]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GXE OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3GXE FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3gxe]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GXE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GXE FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene>, <scene name='pdbligand=HZP:(4S)-4-HYDROXY-L-PROLINE'>HZP</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene>, <scene name='pdbligand=HZP:(4S)-4-HYDROXY-L-PROLINE'>HZP</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3ejh\|3ejh]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3ejh\|3ejh]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FN ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FN ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3gxe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gxe OCA], [~~http~~://pdbe.org/3gxe PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3gxe RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3gxe PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3gxe ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3gxe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gxe OCA], [https://pdbe.org/3gxe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gxe RCSB], [https://www.ebi.ac.uk/pdbsum/3gxe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gxe ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/FINC_HUMAN FINC_HUMAN]] Defects in FN1 are the cause of glomerulopathy with fibronectin deposits type 2 (GFND2) [MIM:[~~http~~://omim.org/entry/601894 601894]]; also known as familial glomerular nephritis with fibronectin deposits or fibronectin glomerulopathy. GFND is a genetically heterogeneous autosomal dominant disorder characterized clinically by proteinuria, microscopic hematuria, and hypertension that leads to end-stage renal failure in the second to fifth decade of life.<ref>PMID:18268355</ref> [[~~http~~://www.uniprot.org/uniprot/CO1A1_HUMAN CO1A1_HUMAN]] Defects in COL1A1 are the cause of Caffey disease (CAFFD) [MIM:[~~http~~://omim.org/entry/114000 114000]]; also known as infantile cortical hyperostosis. Caffey disease is characterized by an infantile episode of massive subperiosteal new bone formation that typically involves the diaphyses of the long bones, mandible, and clavicles. The involved bones may also appear inflamed, with painful swelling and systemic fever often accompanying the illness. The bone changes usually begin before 5 months of age and resolve before 2 years of age.<ref>PMID:8988177</ref> <ref>PMID:12660034</ref> <ref>PMID:15864348</ref> Defects in COL1A1 are a cause of Ehlers-Danlos syndrome type 1 (EDS1) [MIM:[~~http~~://omim.org/entry/130000 130000]]; also known as Ehlers-Danlos syndrome gravis. EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS1 is the severe form of classic Ehlers-Danlos syndrome.<ref>PMID:8988177</ref> <ref>PMID:12660034</ref> <ref>PMID:10739762</ref> <ref>PMID:17211858</ref> Defects in COL1A1 are the cause of Ehlers-Danlos syndrome type 7A (EDS7A) [MIM:[~~http~~://omim.org/entry/130060 130060]]; also known as autosomal dominant Ehlers-Danlos syndrome type VII. EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS7A is marked by bilateral congenital hip dislocation, hyperlaxity of the joints, and recurrent partial dislocations.<ref>PMID:8988177</ref> <ref>PMID:12660034</ref> Defects in COL1A1 are a cause of osteogenesis imperfecta type 1 (OI1) [MIM:[~~http~~://omim.org/entry/166200 166200]]. A dominantly inherited connective tissue disorder characterized by bone fragility and blue sclerae. Osteogenesis imperfecta type 1 is non-deforming with normal height or mild short stature, and no dentinogenesis imperfecta.<ref>PMID:8988177</ref> <ref>PMID:12660034</ref> <ref>PMID:3244312</ref> <ref>PMID:2794057</ref> <ref>PMID:1718984</ref> <ref>PMID:1634225</ref> <ref>PMID:1737847</ref> <ref>PMID:8223589</ref> <ref>PMID:16705691</ref> <ref>PMID:16786509</ref> <ref>PMID:16638323</ref> <ref>PMID:17875077</ref> <ref>PMID:18670065</ref> Defects in COL1A1 are a cause of osteogenesis imperfecta type 2 (OI2) [MIM:[~~http~~://omim.org/entry/166210 166210]]; also known as osteogenesis imperfecta congenita. A connective tissue disorder characterized by bone fragility, with many perinatal fractures, severe bowing of long bones, undermineralization, and death in the perinatal period due to respiratory insufficiency. Defects in COL1A1 are a cause of osteogenesis imperfecta type 3 (OI3) [MIM:[~~http~~://omim.org/entry/259420 259420]]. A connective tissue disorder characterized by progressively deforming bones, very short stature, a triangular face, severe scoliosis, grayish sclera, and dentinogenesis imperfecta. Defects in COL1A1 are a cause of osteogenesis imperfecta type 4 (OI4) [MIM:[~~http~~://omim.org/entry/166220 166220]]; also known as osteogenesis imperfecta with normal sclerae. A connective tissue disorder characterized by moderately short stature, mild to moderate scoliosis, grayish or white sclera and dentinogenesis imperfecta. Genetic variations in COL1A1 are a cause of susceptibility to osteoporosis (OSTEOP) [MIM:[~~http~~://omim.org/entry/166710 166710]]; also known as involutional or senile osteoporosis or postmenopausal osteoporosis. Osteoporosis is characterized by reduced bone mass, disruption of bone microarchitecture without alteration in the composition of bone. Osteoporotic bones are more at risk of fracture.<ref>PMID:8988177</ref> <ref>PMID:12660034</ref> <ref>PMID:8841196</ref> <ref>PMID:9535665</ref> Note=A chromosomal aberration involving COL1A1 is found in dermatofibrosarcoma protuberans. Translocation t(17;22)(q22;q13) with PDGF.<ref>PMID:8988177</ref> <ref>PMID:12660034</ref>	+	[[https://www.uniprot.org/uniprot/FINC_HUMAN FINC_HUMAN]] Defects in FN1 are the cause of glomerulopathy with fibronectin deposits type 2 (GFND2) [MIM:[https://omim.org/entry/601894 601894]]; also known as familial glomerular nephritis with fibronectin deposits or fibronectin glomerulopathy. GFND is a genetically heterogeneous autosomal dominant disorder characterized clinically by proteinuria, microscopic hematuria, and hypertension that leads to end-stage renal failure in the second to fifth decade of life.<ref>PMID:18268355</ref> [[https://www.uniprot.org/uniprot/CO1A1_HUMAN CO1A1_HUMAN]] Defects in COL1A1 are the cause of Caffey disease (CAFFD) [MIM:[https://omim.org/entry/114000 114000]]; also known as infantile cortical hyperostosis. Caffey disease is characterized by an infantile episode of massive subperiosteal new bone formation that typically involves the diaphyses of the long bones, mandible, and clavicles. The involved bones may also appear inflamed, with painful swelling and systemic fever often accompanying the illness. The bone changes usually begin before 5 months of age and resolve before 2 years of age.<ref>PMID:8988177</ref> <ref>PMID:12660034</ref> <ref>PMID:15864348</ref> Defects in COL1A1 are a cause of Ehlers-Danlos syndrome type 1 (EDS1) [MIM:[https://omim.org/entry/130000 130000]]; also known as Ehlers-Danlos syndrome gravis. EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS1 is the severe form of classic Ehlers-Danlos syndrome.<ref>PMID:8988177</ref> <ref>PMID:12660034</ref> <ref>PMID:10739762</ref> <ref>PMID:17211858</ref> Defects in COL1A1 are the cause of Ehlers-Danlos syndrome type 7A (EDS7A) [MIM:[https://omim.org/entry/130060 130060]]; also known as autosomal dominant Ehlers-Danlos syndrome type VII. EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS7A is marked by bilateral congenital hip dislocation, hyperlaxity of the joints, and recurrent partial dislocations.<ref>PMID:8988177</ref> <ref>PMID:12660034</ref> Defects in COL1A1 are a cause of osteogenesis imperfecta type 1 (OI1) [MIM:[https://omim.org/entry/166200 166200]]. A dominantly inherited connective tissue disorder characterized by bone fragility and blue sclerae. Osteogenesis imperfecta type 1 is non-deforming with normal height or mild short stature, and no dentinogenesis imperfecta.<ref>PMID:8988177</ref> <ref>PMID:12660034</ref> <ref>PMID:3244312</ref> <ref>PMID:2794057</ref> <ref>PMID:1718984</ref> <ref>PMID:1634225</ref> <ref>PMID:1737847</ref> <ref>PMID:8223589</ref> <ref>PMID:16705691</ref> <ref>PMID:16786509</ref> <ref>PMID:16638323</ref> <ref>PMID:17875077</ref> <ref>PMID:18670065</ref> Defects in COL1A1 are a cause of osteogenesis imperfecta type 2 (OI2) [MIM:[https://omim.org/entry/166210 166210]]; also known as osteogenesis imperfecta congenita. A connective tissue disorder characterized by bone fragility, with many perinatal fractures, severe bowing of long bones, undermineralization, and death in the perinatal period due to respiratory insufficiency. Defects in COL1A1 are a cause of osteogenesis imperfecta type 3 (OI3) [MIM:[https://omim.org/entry/259420 259420]]. A connective tissue disorder characterized by progressively deforming bones, very short stature, a triangular face, severe scoliosis, grayish sclera, and dentinogenesis imperfecta. Defects in COL1A1 are a cause of osteogenesis imperfecta type 4 (OI4) [MIM:[https://omim.org/entry/166220 166220]]; also known as osteogenesis imperfecta with normal sclerae. A connective tissue disorder characterized by moderately short stature, mild to moderate scoliosis, grayish or white sclera and dentinogenesis imperfecta. Genetic variations in COL1A1 are a cause of susceptibility to osteoporosis (OSTEOP) [MIM:[https://omim.org/entry/166710 166710]]; also known as involutional or senile osteoporosis or postmenopausal osteoporosis. Osteoporosis is characterized by reduced bone mass, disruption of bone microarchitecture without alteration in the composition of bone. Osteoporotic bones are more at risk of fracture.<ref>PMID:8988177</ref> <ref>PMID:12660034</ref> <ref>PMID:8841196</ref> <ref>PMID:9535665</ref> Note=A chromosomal aberration involving COL1A1 is found in dermatofibrosarcoma protuberans. Translocation t(17;22)(q22;q13) with PDGF.<ref>PMID:8988177</ref> <ref>PMID:12660034</ref>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/FINC_HUMAN FINC_HUMAN]] Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape.<ref>PMID:8114919</ref> <ref>PMID:11209058</ref> <ref>PMID:15665290</ref> <ref>PMID:19379667</ref> Anastellin binds fibronectin and induces fibril formation. This fibronectin polymer, named superfibronectin, exhibits enhanced adhesive properties. Both anastellin and superfibronectin inhibit tumor growth, angiogenesis and metastasis. Anastellin activates p38 MAPK and inhibits lysophospholipid signaling.<ref>PMID:8114919</ref> <ref>PMID:11209058</ref> <ref>PMID:15665290</ref> <ref>PMID:19379667</ref> [[~~http~~://www.uniprot.org/uniprot/CO1A1_HUMAN CO1A1_HUMAN]] Type I collagen is a member of group I collagen (fibrillar forming collagen).	+	[[https://www.uniprot.org/uniprot/FINC_HUMAN FINC_HUMAN]] Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape.<ref>PMID:8114919</ref> <ref>PMID:11209058</ref> <ref>PMID:15665290</ref> <ref>PMID:19379667</ref> Anastellin binds fibronectin and induces fibril formation. This fibronectin polymer, named superfibronectin, exhibits enhanced adhesive properties. Both anastellin and superfibronectin inhibit tumor growth, angiogenesis and metastasis. Anastellin activates p38 MAPK and inhibits lysophospholipid signaling.<ref>PMID:8114919</ref> <ref>PMID:11209058</ref> <ref>PMID:15665290</ref> <ref>PMID:19379667</ref> [[https://www.uniprot.org/uniprot/CO1A1_HUMAN CO1A1_HUMAN]] Type I collagen is a member of group I collagen (fibrillar forming collagen).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 35:		Line 35:

	==See Also==		==See Also==
-	*[[Collagen\|Collagen]]	+	*[[Collagen 3D structures\|Collagen 3D structures]]
-	*[[Fibronectin\|Fibronectin]]	+	*[[Fibronectin 3D structures\|Fibronectin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 42:		Line 42:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Campbell, I D]]		[[Category: Campbell, I D]]
	[[Category: Sladek, B]]		[[Category: Sladek, B]]

OCA at 05:45, 7 December 2018

OCA — Fri, 07 Dec 2018 05:45:09 GMT

←Older revision		Revision as of 05:45, 7 December 2018
Line 18:		Line 18:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gx/3gxe_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gx/3gxe_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>

OCA at 08:42, 5 August 2016

OCA — Fri, 05 Aug 2016 08:42:05 GMT

←Older revision		Revision as of 08:42, 5 August 2016
Line 1:		Line 1:
		+
	==Complex of a Low Affinity Collagen Site with the Fibronectin 8-9FnI Domain Pair==		==Complex of a Low Affinity Collagen Site with the Fibronectin 8-9FnI Domain Pair==
	<StructureSection load='3gxe' size='340' side='right' caption='[[3gxe]], [[Resolution\|resolution]] 2.60Å' scene=''>		<StructureSection load='3gxe' size='340' side='right' caption='[[3gxe]], [[Resolution\|resolution]] 2.60Å' scene=''>
Line 7:		Line 8:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3ejh\|3ejh]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3ejh\|3ejh]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3gxe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gxe OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3gxe RCSB], [http://www.ebi.ac.uk/pdbsum/3gxe PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3gxe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gxe OCA], [http://pdbe.org/3gxe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3gxe RCSB], [http://www.ebi.ac.uk/pdbsum/3gxe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3gxe ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 21:		Line 22:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3gxe ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 31:		Line 32:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 3gxe" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 17:10, 21 December 2014

OCA — Sun, 21 Dec 2014 17:10:22 GMT

←Older revision		Revision as of 17:10, 21 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3gxe\| PDB=3gxe \| SCENE= }}~~	+	==Complex of a Low Affinity Collagen Site with the Fibronectin 8-9FnI Domain Pair==
-	===Complex of a Low Affinity Collagen Site with the Fibronectin 8-9FnI Domain Pair===	+	<StructureSection load='3gxe' size='340' side='right' caption='[[3gxe]], [[Resolution\|resolution]] 2.60Å' scene=''>
-	~~{{ABSTRACT_PUBMED_23653354}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[3gxe]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GXE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3GXE FirstGlance]. <br>
-	==Disease==	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
		+	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene>, <scene name='pdbligand=HZP:(4S)-4-HYDROXY-L-PROLINE'>HZP</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3ejh\|3ejh]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3gxe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gxe OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3gxe RCSB], [http://www.ebi.ac.uk/pdbsum/3gxe PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
	[[http://www.uniprot.org/uniprot/FINC_HUMAN FINC_HUMAN]] Defects in FN1 are the cause of glomerulopathy with fibronectin deposits type 2 (GFND2) [MIM:[http://omim.org/entry/601894 601894]]; also known as familial glomerular nephritis with fibronectin deposits or fibronectin glomerulopathy. GFND is a genetically heterogeneous autosomal dominant disorder characterized clinically by proteinuria, microscopic hematuria, and hypertension that leads to end-stage renal failure in the second to fifth decade of life.<ref>PMID:18268355</ref> [[http://www.uniprot.org/uniprot/CO1A1_HUMAN CO1A1_HUMAN]] Defects in COL1A1 are the cause of Caffey disease (CAFFD) [MIM:[http://omim.org/entry/114000 114000]]; also known as infantile cortical hyperostosis. Caffey disease is characterized by an infantile episode of massive subperiosteal new bone formation that typically involves the diaphyses of the long bones, mandible, and clavicles. The involved bones may also appear inflamed, with painful swelling and systemic fever often accompanying the illness. The bone changes usually begin before 5 months of age and resolve before 2 years of age.<ref>PMID:8988177</ref> <ref>PMID:12660034</ref> <ref>PMID:15864348</ref> Defects in COL1A1 are a cause of Ehlers-Danlos syndrome type 1 (EDS1) [MIM:[http://omim.org/entry/130000 130000]]; also known as Ehlers-Danlos syndrome gravis. EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS1 is the severe form of classic Ehlers-Danlos syndrome.<ref>PMID:8988177</ref> <ref>PMID:12660034</ref> <ref>PMID:10739762</ref> <ref>PMID:17211858</ref> Defects in COL1A1 are the cause of Ehlers-Danlos syndrome type 7A (EDS7A) [MIM:[http://omim.org/entry/130060 130060]]; also known as autosomal dominant Ehlers-Danlos syndrome type VII. EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS7A is marked by bilateral congenital hip dislocation, hyperlaxity of the joints, and recurrent partial dislocations.<ref>PMID:8988177</ref> <ref>PMID:12660034</ref> Defects in COL1A1 are a cause of osteogenesis imperfecta type 1 (OI1) [MIM:[http://omim.org/entry/166200 166200]]. A dominantly inherited connective tissue disorder characterized by bone fragility and blue sclerae. Osteogenesis imperfecta type 1 is non-deforming with normal height or mild short stature, and no dentinogenesis imperfecta.<ref>PMID:8988177</ref> <ref>PMID:12660034</ref> <ref>PMID:3244312</ref> <ref>PMID:2794057</ref> <ref>PMID:1718984</ref> <ref>PMID:1634225</ref> <ref>PMID:1737847</ref> <ref>PMID:8223589</ref> <ref>PMID:16705691</ref> <ref>PMID:16786509</ref> <ref>PMID:16638323</ref> <ref>PMID:17875077</ref> <ref>PMID:18670065</ref> Defects in COL1A1 are a cause of osteogenesis imperfecta type 2 (OI2) [MIM:[http://omim.org/entry/166210 166210]]; also known as osteogenesis imperfecta congenita. A connective tissue disorder characterized by bone fragility, with many perinatal fractures, severe bowing of long bones, undermineralization, and death in the perinatal period due to respiratory insufficiency. Defects in COL1A1 are a cause of osteogenesis imperfecta type 3 (OI3) [MIM:[http://omim.org/entry/259420 259420]]. A connective tissue disorder characterized by progressively deforming bones, very short stature, a triangular face, severe scoliosis, grayish sclera, and dentinogenesis imperfecta. Defects in COL1A1 are a cause of osteogenesis imperfecta type 4 (OI4) [MIM:[http://omim.org/entry/166220 166220]]; also known as osteogenesis imperfecta with normal sclerae. A connective tissue disorder characterized by moderately short stature, mild to moderate scoliosis, grayish or white sclera and dentinogenesis imperfecta. Genetic variations in COL1A1 are a cause of susceptibility to osteoporosis (OSTEOP) [MIM:[http://omim.org/entry/166710 166710]]; also known as involutional or senile osteoporosis or postmenopausal osteoporosis. Osteoporosis is characterized by reduced bone mass, disruption of bone microarchitecture without alteration in the composition of bone. Osteoporotic bones are more at risk of fracture.<ref>PMID:8988177</ref> <ref>PMID:12660034</ref> <ref>PMID:8841196</ref> <ref>PMID:9535665</ref> Note=A chromosomal aberration involving COL1A1 is found in dermatofibrosarcoma protuberans. Translocation t(17;22)(q22;q13) with PDGF.<ref>PMID:8988177</ref> <ref>PMID:12660034</ref>		[[http://www.uniprot.org/uniprot/FINC_HUMAN FINC_HUMAN]] Defects in FN1 are the cause of glomerulopathy with fibronectin deposits type 2 (GFND2) [MIM:[http://omim.org/entry/601894 601894]]; also known as familial glomerular nephritis with fibronectin deposits or fibronectin glomerulopathy. GFND is a genetically heterogeneous autosomal dominant disorder characterized clinically by proteinuria, microscopic hematuria, and hypertension that leads to end-stage renal failure in the second to fifth decade of life.<ref>PMID:18268355</ref> [[http://www.uniprot.org/uniprot/CO1A1_HUMAN CO1A1_HUMAN]] Defects in COL1A1 are the cause of Caffey disease (CAFFD) [MIM:[http://omim.org/entry/114000 114000]]; also known as infantile cortical hyperostosis. Caffey disease is characterized by an infantile episode of massive subperiosteal new bone formation that typically involves the diaphyses of the long bones, mandible, and clavicles. The involved bones may also appear inflamed, with painful swelling and systemic fever often accompanying the illness. The bone changes usually begin before 5 months of age and resolve before 2 years of age.<ref>PMID:8988177</ref> <ref>PMID:12660034</ref> <ref>PMID:15864348</ref> Defects in COL1A1 are a cause of Ehlers-Danlos syndrome type 1 (EDS1) [MIM:[http://omim.org/entry/130000 130000]]; also known as Ehlers-Danlos syndrome gravis. EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS1 is the severe form of classic Ehlers-Danlos syndrome.<ref>PMID:8988177</ref> <ref>PMID:12660034</ref> <ref>PMID:10739762</ref> <ref>PMID:17211858</ref> Defects in COL1A1 are the cause of Ehlers-Danlos syndrome type 7A (EDS7A) [MIM:[http://omim.org/entry/130060 130060]]; also known as autosomal dominant Ehlers-Danlos syndrome type VII. EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS7A is marked by bilateral congenital hip dislocation, hyperlaxity of the joints, and recurrent partial dislocations.<ref>PMID:8988177</ref> <ref>PMID:12660034</ref> Defects in COL1A1 are a cause of osteogenesis imperfecta type 1 (OI1) [MIM:[http://omim.org/entry/166200 166200]]. A dominantly inherited connective tissue disorder characterized by bone fragility and blue sclerae. Osteogenesis imperfecta type 1 is non-deforming with normal height or mild short stature, and no dentinogenesis imperfecta.<ref>PMID:8988177</ref> <ref>PMID:12660034</ref> <ref>PMID:3244312</ref> <ref>PMID:2794057</ref> <ref>PMID:1718984</ref> <ref>PMID:1634225</ref> <ref>PMID:1737847</ref> <ref>PMID:8223589</ref> <ref>PMID:16705691</ref> <ref>PMID:16786509</ref> <ref>PMID:16638323</ref> <ref>PMID:17875077</ref> <ref>PMID:18670065</ref> Defects in COL1A1 are a cause of osteogenesis imperfecta type 2 (OI2) [MIM:[http://omim.org/entry/166210 166210]]; also known as osteogenesis imperfecta congenita. A connective tissue disorder characterized by bone fragility, with many perinatal fractures, severe bowing of long bones, undermineralization, and death in the perinatal period due to respiratory insufficiency. Defects in COL1A1 are a cause of osteogenesis imperfecta type 3 (OI3) [MIM:[http://omim.org/entry/259420 259420]]. A connective tissue disorder characterized by progressively deforming bones, very short stature, a triangular face, severe scoliosis, grayish sclera, and dentinogenesis imperfecta. Defects in COL1A1 are a cause of osteogenesis imperfecta type 4 (OI4) [MIM:[http://omim.org/entry/166220 166220]]; also known as osteogenesis imperfecta with normal sclerae. A connective tissue disorder characterized by moderately short stature, mild to moderate scoliosis, grayish or white sclera and dentinogenesis imperfecta. Genetic variations in COL1A1 are a cause of susceptibility to osteoporosis (OSTEOP) [MIM:[http://omim.org/entry/166710 166710]]; also known as involutional or senile osteoporosis or postmenopausal osteoporosis. Osteoporosis is characterized by reduced bone mass, disruption of bone microarchitecture without alteration in the composition of bone. Osteoporotic bones are more at risk of fracture.<ref>PMID:8988177</ref> <ref>PMID:12660034</ref> <ref>PMID:8841196</ref> <ref>PMID:9535665</ref> Note=A chromosomal aberration involving COL1A1 is found in dermatofibrosarcoma protuberans. Translocation t(17;22)(q22;q13) with PDGF.<ref>PMID:8988177</ref> <ref>PMID:12660034</ref>
-		+	== Function ==
-	==Function==	+
	[[http://www.uniprot.org/uniprot/FINC_HUMAN FINC_HUMAN]] Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape.<ref>PMID:8114919</ref> <ref>PMID:11209058</ref> <ref>PMID:15665290</ref> <ref>PMID:19379667</ref> Anastellin binds fibronectin and induces fibril formation. This fibronectin polymer, named superfibronectin, exhibits enhanced adhesive properties. Both anastellin and superfibronectin inhibit tumor growth, angiogenesis and metastasis. Anastellin activates p38 MAPK and inhibits lysophospholipid signaling.<ref>PMID:8114919</ref> <ref>PMID:11209058</ref> <ref>PMID:15665290</ref> <ref>PMID:19379667</ref> [[http://www.uniprot.org/uniprot/CO1A1_HUMAN CO1A1_HUMAN]] Type I collagen is a member of group I collagen (fibrillar forming collagen).		[[http://www.uniprot.org/uniprot/FINC_HUMAN FINC_HUMAN]] Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape.<ref>PMID:8114919</ref> <ref>PMID:11209058</ref> <ref>PMID:15665290</ref> <ref>PMID:19379667</ref> Anastellin binds fibronectin and induces fibril formation. This fibronectin polymer, named superfibronectin, exhibits enhanced adhesive properties. Both anastellin and superfibronectin inhibit tumor growth, angiogenesis and metastasis. Anastellin activates p38 MAPK and inhibits lysophospholipid signaling.<ref>PMID:8114919</ref> <ref>PMID:11209058</ref> <ref>PMID:15665290</ref> <ref>PMID:19379667</ref> [[http://www.uniprot.org/uniprot/CO1A1_HUMAN CO1A1_HUMAN]] Type I collagen is a member of group I collagen (fibrillar forming collagen).
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gx/3gxe_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Despite its biological importance, the interaction between fibronectin (FN) and collagen, two abundant and crucial tissue components, has not been well characterized on a structural level. Here, we analyzed the four interactions formed between epitopes of collagen type I and the collagen-binding fragment (gelatin-binding domain (GBD)) of human FN using solution NMR, fluorescence, and small angle x-ray scattering methods. Collagen association with FN modules (8-9)FnI occurs through a conserved structural mechanism but exhibits a 400-fold disparity in affinity between collagen sites. This disparity is reduced in the full-length GBD, as (6)FnI(1-2)FnII(7)FnI binds a specific collagen epitope next to the weakest (8-9)FnI-binding site. The cooperative engagement of all GBD modules with collagen results in four broadly equipotent FN-collagen interaction sites. Collagen association stabilizes a distinct monomeric GBD conformation in solution, giving further evidence to the view that FN fragments form well defined functional and structural units.

-	~~==About this Structure==~~	+	Structural analysis of collagen type I interactions with human fibronectin reveals a cooperative binding mode.,Erat MC, Sladek B, Campbell ID, Vakonakis I J Biol Chem. 2013 Jun 14;288(24):17441-50. doi: 10.1074/jbc.M113.469841. Epub, 2013 May 6. PMID:23653354<ref>PMID:23653354</ref>
-	~~[[3gxe]] is a 4 chain structure~~ with ~~sequence from [http~~:~~//en~~.~~wikipedia~~.~~org~~/~~wiki/Human Human]~~. ~~Full crystallographic information is available from [http~~://~~oca~~.~~weizmann~~.ac.il/~~oca-bin/ocashort?id=3GXE OCA].~~	+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

	==See Also==		==See Also==
	*[[Collagen\|Collagen]]		*[[Collagen\|Collagen]]
	*[[Fibronectin\|Fibronectin]]		*[[Fibronectin\|Fibronectin]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:023653354</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Human]]		[[Category: Human]]
-	[[Category: Campbell, I D.]]	+	[[Category: Campbell, I D]]
-	[[Category: Sladek, B.]]	+	[[Category: Sladek, B]]
-	[[Category: Vakonakis, I.]]	+	[[Category: Vakonakis, I]]
	[[Category: Cell adhesion]]		[[Category: Cell adhesion]]
	[[Category: Protein-peptide complex]]		[[Category: Protein-peptide complex]]

OCA at 06:00, 29 January 2014

OCA — Wed, 29 Jan 2014 06:00:09 GMT

←Older revision		Revision as of 06:00, 29 January 2014
Line 1:		Line 1:
	{{STRUCTURE_3gxe\| PDB=3gxe \| SCENE= }}		{{STRUCTURE_3gxe\| PDB=3gxe \| SCENE= }}
	===Complex of a Low Affinity Collagen Site with the Fibronectin 8-9FnI Domain Pair===		===Complex of a Low Affinity Collagen Site with the Fibronectin 8-9FnI Domain Pair===
		+	{{ABSTRACT_PUBMED_23653354}}

	==Disease==		==Disease==
Line 9:		Line 10:

	==About this Structure==		==About this Structure==
-	[[3gxe]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GXE OCA].	+	[[3gxe]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GXE OCA].

	==See Also==		==See Also==
Line 16:		Line 17:

	==Reference==		==Reference==
-	<references group="xtra"/><references/>	+	<ref group="xtra">PMID:023653354</ref><references group="xtra"/><references/>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Campbell, I D.]]		[[Category: Campbell, I D.]]
	[[Category: Sladek, B.]]		[[Category: Sladek, B.]]

OCA at 06:19, 16 May 2013

OCA — Thu, 16 May 2013 06:19:36 GMT

←Older revision		Revision as of 06:19, 16 May 2013
Line 3:		Line 3:

	==Disease==		==Disease==
-	[[http://www.uniprot.org/uniprot/FINC_HUMAN FINC_HUMAN]] Defects in FN1 are the cause of glomerulopathy with fibronectin deposits type 2 (GFND2) [MIM:[http://omim.org/entry/601894 601894]]; also known as familial glomerular nephritis with fibronectin deposits or fibronectin glomerulopathy. GFND is a genetically heterogeneous autosomal dominant disorder characterized clinically by proteinuria, microscopic hematuria, and hypertension that leads to end-stage renal failure in the second to fifth decade of life.<ref>PMID:18268355</ref> [[http://www.uniprot.org/uniprot/CO1A1_HUMAN CO1A1_HUMAN]] Defects in COL1A1 are the cause of Caffey disease (CAFFD) [MIM:[http://omim.org/entry/114000 114000]]; also known as infantile cortical hyperostosis. Caffey disease is characterized by an infantile episode of massive subperiosteal new bone formation that typically involves the diaphyses of the long bones, mandible, and clavicles. The involved bones may also appear inflamed, with painful swelling and systemic fever often accompanying the illness. The bone changes usually begin before 5 months of age and resolve before 2 years of age.<ref>PMID:8988177</ref><ref>PMID:12660034</ref><ref>PMID:15864348</ref> Defects in COL1A1 are a cause of Ehlers-Danlos syndrome type 1 (EDS1) [MIM:[http://omim.org/entry/130000 130000]]; also known as Ehlers-Danlos syndrome gravis. EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS1 is the severe form of classic Ehlers-Danlos syndrome.<ref>PMID:8988177</ref><ref>PMID:12660034</ref><ref>PMID:10739762</ref><ref>PMID:17211858</ref> Defects in COL1A1 are the cause of Ehlers-Danlos syndrome type 7A (EDS7A) [MIM:[http://omim.org/entry/130060 130060]]; also known as autosomal dominant Ehlers-Danlos syndrome type VII. EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS7A is marked by bilateral congenital hip dislocation, hyperlaxity of the joints, and recurrent partial dislocations.<ref>PMID:8988177</ref><ref>PMID:12660034</ref> Defects in COL1A1 are a cause of osteogenesis imperfecta type 1 (OI1) [MIM:[http://omim.org/entry/166200 166200]]. A dominantly inherited connective tissue disorder characterized by bone fragility and blue sclerae. Osteogenesis imperfecta type 1 is non-deforming with normal height or mild short stature, and no dentinogenesis imperfecta.<ref>PMID:8988177</ref><ref>PMID:12660034</ref><ref>PMID:3244312</ref><ref>PMID:2794057</ref><ref>PMID:1718984</ref><ref>PMID:1634225</ref><ref>PMID:1737847</ref><ref>PMID:8223589</ref><ref>PMID:16705691</ref><ref>PMID:16786509</ref><ref>PMID:16638323</ref><ref>PMID:17875077</ref><ref>PMID:18670065</ref> Defects in COL1A1 are a cause of osteogenesis imperfecta type 2 (OI2) [MIM:[http://omim.org/entry/166210 166210]]; also known as osteogenesis imperfecta congenita. A connective tissue disorder characterized by bone fragility, with many perinatal fractures, severe bowing of long bones, undermineralization, and death in the perinatal period due to respiratory insufficiency. Defects in COL1A1 are a cause of osteogenesis imperfecta type 3 (OI3) [MIM:[http://omim.org/entry/259420 259420]]. A connective tissue disorder characterized by progressively deforming bones, very short stature, a triangular face, severe scoliosis, grayish sclera, and dentinogenesis imperfecta. Defects in COL1A1 are a cause of osteogenesis imperfecta type 4 (OI4) [MIM:[http://omim.org/entry/166220 166220]]; also known as osteogenesis imperfecta with normal sclerae. A connective tissue disorder characterized by moderately short stature, mild to moderate scoliosis, grayish or white sclera and dentinogenesis imperfecta. Genetic variations in COL1A1 are a cause of susceptibility to osteoporosis (OSTEOP) [MIM:[http://omim.org/entry/166710 166710]]; also known as involutional or senile osteoporosis or postmenopausal osteoporosis. Osteoporosis is characterized by reduced bone mass, disruption of bone microarchitecture without alteration in the composition of bone. Osteoporotic bones are more at risk of fracture.<ref>PMID:8988177</ref><ref>PMID:12660034</ref><ref>PMID:8841196</ref><ref>PMID:9535665</ref> Note=A chromosomal aberration involving COL1A1 is found in dermatofibrosarcoma protuberans. Translocation t(17;22)(q22;q13) with PDGF.<ref>PMID:8988177</ref><ref>PMID:12660034</ref>	+	[[http://www.uniprot.org/uniprot/FINC_HUMAN FINC_HUMAN]] Defects in FN1 are the cause of glomerulopathy with fibronectin deposits type 2 (GFND2) [MIM:[http://omim.org/entry/601894 601894]]; also known as familial glomerular nephritis with fibronectin deposits or fibronectin glomerulopathy. GFND is a genetically heterogeneous autosomal dominant disorder characterized clinically by proteinuria, microscopic hematuria, and hypertension that leads to end-stage renal failure in the second to fifth decade of life.<ref>PMID:18268355</ref> [[http://www.uniprot.org/uniprot/CO1A1_HUMAN CO1A1_HUMAN]] Defects in COL1A1 are the cause of Caffey disease (CAFFD) [MIM:[http://omim.org/entry/114000 114000]]; also known as infantile cortical hyperostosis. Caffey disease is characterized by an infantile episode of massive subperiosteal new bone formation that typically involves the diaphyses of the long bones, mandible, and clavicles. The involved bones may also appear inflamed, with painful swelling and systemic fever often accompanying the illness. The bone changes usually begin before 5 months of age and resolve before 2 years of age.<ref>PMID:8988177</ref> <ref>PMID:12660034</ref> <ref>PMID:15864348</ref> Defects in COL1A1 are a cause of Ehlers-Danlos syndrome type 1 (EDS1) [MIM:[http://omim.org/entry/130000 130000]]; also known as Ehlers-Danlos syndrome gravis. EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS1 is the severe form of classic Ehlers-Danlos syndrome.<ref>PMID:8988177</ref> <ref>PMID:12660034</ref> <ref>PMID:10739762</ref> <ref>PMID:17211858</ref> Defects in COL1A1 are the cause of Ehlers-Danlos syndrome type 7A (EDS7A) [MIM:[http://omim.org/entry/130060 130060]]; also known as autosomal dominant Ehlers-Danlos syndrome type VII. EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS7A is marked by bilateral congenital hip dislocation, hyperlaxity of the joints, and recurrent partial dislocations.<ref>PMID:8988177</ref> <ref>PMID:12660034</ref> Defects in COL1A1 are a cause of osteogenesis imperfecta type 1 (OI1) [MIM:[http://omim.org/entry/166200 166200]]. A dominantly inherited connective tissue disorder characterized by bone fragility and blue sclerae. Osteogenesis imperfecta type 1 is non-deforming with normal height or mild short stature, and no dentinogenesis imperfecta.<ref>PMID:8988177</ref> <ref>PMID:12660034</ref> <ref>PMID:3244312</ref> <ref>PMID:2794057</ref> <ref>PMID:1718984</ref> <ref>PMID:1634225</ref> <ref>PMID:1737847</ref> <ref>PMID:8223589</ref> <ref>PMID:16705691</ref> <ref>PMID:16786509</ref> <ref>PMID:16638323</ref> <ref>PMID:17875077</ref> <ref>PMID:18670065</ref> Defects in COL1A1 are a cause of osteogenesis imperfecta type 2 (OI2) [MIM:[http://omim.org/entry/166210 166210]]; also known as osteogenesis imperfecta congenita. A connective tissue disorder characterized by bone fragility, with many perinatal fractures, severe bowing of long bones, undermineralization, and death in the perinatal period due to respiratory insufficiency. Defects in COL1A1 are a cause of osteogenesis imperfecta type 3 (OI3) [MIM:[http://omim.org/entry/259420 259420]]. A connective tissue disorder characterized by progressively deforming bones, very short stature, a triangular face, severe scoliosis, grayish sclera, and dentinogenesis imperfecta. Defects in COL1A1 are a cause of osteogenesis imperfecta type 4 (OI4) [MIM:[http://omim.org/entry/166220 166220]]; also known as osteogenesis imperfecta with normal sclerae. A connective tissue disorder characterized by moderately short stature, mild to moderate scoliosis, grayish or white sclera and dentinogenesis imperfecta. Genetic variations in COL1A1 are a cause of susceptibility to osteoporosis (OSTEOP) [MIM:[http://omim.org/entry/166710 166710]]; also known as involutional or senile osteoporosis or postmenopausal osteoporosis. Osteoporosis is characterized by reduced bone mass, disruption of bone microarchitecture without alteration in the composition of bone. Osteoporotic bones are more at risk of fracture.<ref>PMID:8988177</ref> <ref>PMID:12660034</ref> <ref>PMID:8841196</ref> <ref>PMID:9535665</ref> Note=A chromosomal aberration involving COL1A1 is found in dermatofibrosarcoma protuberans. Translocation t(17;22)(q22;q13) with PDGF.<ref>PMID:8988177</ref> <ref>PMID:12660034</ref>

	==Function==		==Function==
-	[[http://www.uniprot.org/uniprot/FINC_HUMAN FINC_HUMAN]] Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape.<ref>PMID:8114919</ref><ref>PMID:11209058</ref><ref>PMID:15665290</ref><ref>PMID:19379667</ref> Anastellin binds fibronectin and induces fibril formation. This fibronectin polymer, named superfibronectin, exhibits enhanced adhesive properties. Both anastellin and superfibronectin inhibit tumor growth, angiogenesis and metastasis. Anastellin activates p38 MAPK and inhibits lysophospholipid signaling.<ref>PMID:8114919</ref><ref>PMID:11209058</ref><ref>PMID:15665290</ref><ref>PMID:19379667</ref> [[http://www.uniprot.org/uniprot/CO1A1_HUMAN CO1A1_HUMAN]] Type I collagen is a member of group I collagen (fibrillar forming collagen).	+	[[http://www.uniprot.org/uniprot/FINC_HUMAN FINC_HUMAN]] Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape.<ref>PMID:8114919</ref> <ref>PMID:11209058</ref> <ref>PMID:15665290</ref> <ref>PMID:19379667</ref> Anastellin binds fibronectin and induces fibril formation. This fibronectin polymer, named superfibronectin, exhibits enhanced adhesive properties. Both anastellin and superfibronectin inhibit tumor growth, angiogenesis and metastasis. Anastellin activates p38 MAPK and inhibits lysophospholipid signaling.<ref>PMID:8114919</ref> <ref>PMID:11209058</ref> <ref>PMID:15665290</ref> <ref>PMID:19379667</ref> [[http://www.uniprot.org/uniprot/CO1A1_HUMAN CO1A1_HUMAN]] Type I collagen is a member of group I collagen (fibrillar forming collagen).

	==About this Structure==		==About this Structure==

OCA at 18:48, 24 March 2013

OCA — Sun, 24 Mar 2013 18:48:55 GMT

←Older revision		Revision as of 18:48, 24 March 2013
Line 1:		Line 1:
-	[[Image:3gxe.png\|left\|200px]]
-
	{{STRUCTURE_3gxe\| PDB=3gxe \| SCENE= }}		{{STRUCTURE_3gxe\| PDB=3gxe \| SCENE= }}
-
	===Complex of a Low Affinity Collagen Site with the Fibronectin 8-9FnI Domain Pair===		===Complex of a Low Affinity Collagen Site with the Fibronectin 8-9FnI Domain Pair===

		+	==Disease==
		+	[[http://www.uniprot.org/uniprot/FINC_HUMAN FINC_HUMAN]] Defects in FN1 are the cause of glomerulopathy with fibronectin deposits type 2 (GFND2) [MIM:[http://omim.org/entry/601894 601894]]; also known as familial glomerular nephritis with fibronectin deposits or fibronectin glomerulopathy. GFND is a genetically heterogeneous autosomal dominant disorder characterized clinically by proteinuria, microscopic hematuria, and hypertension that leads to end-stage renal failure in the second to fifth decade of life.<ref>PMID:18268355</ref> [[http://www.uniprot.org/uniprot/CO1A1_HUMAN CO1A1_HUMAN]] Defects in COL1A1 are the cause of Caffey disease (CAFFD) [MIM:[http://omim.org/entry/114000 114000]]; also known as infantile cortical hyperostosis. Caffey disease is characterized by an infantile episode of massive subperiosteal new bone formation that typically involves the diaphyses of the long bones, mandible, and clavicles. The involved bones may also appear inflamed, with painful swelling and systemic fever often accompanying the illness. The bone changes usually begin before 5 months of age and resolve before 2 years of age.<ref>PMID:8988177</ref><ref>PMID:12660034</ref><ref>PMID:15864348</ref> Defects in COL1A1 are a cause of Ehlers-Danlos syndrome type 1 (EDS1) [MIM:[http://omim.org/entry/130000 130000]]; also known as Ehlers-Danlos syndrome gravis. EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS1 is the severe form of classic Ehlers-Danlos syndrome.<ref>PMID:8988177</ref><ref>PMID:12660034</ref><ref>PMID:10739762</ref><ref>PMID:17211858</ref> Defects in COL1A1 are the cause of Ehlers-Danlos syndrome type 7A (EDS7A) [MIM:[http://omim.org/entry/130060 130060]]; also known as autosomal dominant Ehlers-Danlos syndrome type VII. EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS7A is marked by bilateral congenital hip dislocation, hyperlaxity of the joints, and recurrent partial dislocations.<ref>PMID:8988177</ref><ref>PMID:12660034</ref> Defects in COL1A1 are a cause of osteogenesis imperfecta type 1 (OI1) [MIM:[http://omim.org/entry/166200 166200]]. A dominantly inherited connective tissue disorder characterized by bone fragility and blue sclerae. Osteogenesis imperfecta type 1 is non-deforming with normal height or mild short stature, and no dentinogenesis imperfecta.<ref>PMID:8988177</ref><ref>PMID:12660034</ref><ref>PMID:3244312</ref><ref>PMID:2794057</ref><ref>PMID:1718984</ref><ref>PMID:1634225</ref><ref>PMID:1737847</ref><ref>PMID:8223589</ref><ref>PMID:16705691</ref><ref>PMID:16786509</ref><ref>PMID:16638323</ref><ref>PMID:17875077</ref><ref>PMID:18670065</ref> Defects in COL1A1 are a cause of osteogenesis imperfecta type 2 (OI2) [MIM:[http://omim.org/entry/166210 166210]]; also known as osteogenesis imperfecta congenita. A connective tissue disorder characterized by bone fragility, with many perinatal fractures, severe bowing of long bones, undermineralization, and death in the perinatal period due to respiratory insufficiency. Defects in COL1A1 are a cause of osteogenesis imperfecta type 3 (OI3) [MIM:[http://omim.org/entry/259420 259420]]. A connective tissue disorder characterized by progressively deforming bones, very short stature, a triangular face, severe scoliosis, grayish sclera, and dentinogenesis imperfecta. Defects in COL1A1 are a cause of osteogenesis imperfecta type 4 (OI4) [MIM:[http://omim.org/entry/166220 166220]]; also known as osteogenesis imperfecta with normal sclerae. A connective tissue disorder characterized by moderately short stature, mild to moderate scoliosis, grayish or white sclera and dentinogenesis imperfecta. Genetic variations in COL1A1 are a cause of susceptibility to osteoporosis (OSTEOP) [MIM:[http://omim.org/entry/166710 166710]]; also known as involutional or senile osteoporosis or postmenopausal osteoporosis. Osteoporosis is characterized by reduced bone mass, disruption of bone microarchitecture without alteration in the composition of bone. Osteoporotic bones are more at risk of fracture.<ref>PMID:8988177</ref><ref>PMID:12660034</ref><ref>PMID:8841196</ref><ref>PMID:9535665</ref> Note=A chromosomal aberration involving COL1A1 is found in dermatofibrosarcoma protuberans. Translocation t(17;22)(q22;q13) with PDGF.<ref>PMID:8988177</ref><ref>PMID:12660034</ref>
		+
		+	==Function==
		+	[[http://www.uniprot.org/uniprot/FINC_HUMAN FINC_HUMAN]] Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape.<ref>PMID:8114919</ref><ref>PMID:11209058</ref><ref>PMID:15665290</ref><ref>PMID:19379667</ref> Anastellin binds fibronectin and induces fibril formation. This fibronectin polymer, named superfibronectin, exhibits enhanced adhesive properties. Both anastellin and superfibronectin inhibit tumor growth, angiogenesis and metastasis. Anastellin activates p38 MAPK and inhibits lysophospholipid signaling.<ref>PMID:8114919</ref><ref>PMID:11209058</ref><ref>PMID:15665290</ref><ref>PMID:19379667</ref> [[http://www.uniprot.org/uniprot/CO1A1_HUMAN CO1A1_HUMAN]] Type I collagen is a member of group I collagen (fibrillar forming collagen).

	==About this Structure==		==About this Structure==
Line 12:		Line 14:
	*[[Collagen\|Collagen]]		*[[Collagen\|Collagen]]
	*[[Fibronectin\|Fibronectin]]		*[[Fibronectin\|Fibronectin]]
		+
		+	==Reference==
		+	<references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Campbell, I D.]]		[[Category: Campbell, I D.]]

OCA at 19:23, 20 October 2012

OCA — Sat, 20 Oct 2012 19:23:32 GMT

←Older revision		Revision as of 19:23, 20 October 2012
Line 7:		Line 7:

	==About this Structure==		==About this Structure==
-	[[3gxe]] is a 4 chain structure ~~of [[Collagen]] and [[Fibronectin]]~~ with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GXE OCA].	+	[[3gxe]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GXE OCA].

	==See Also==		==See Also==

OCA at 07:11, 27 July 2012

OCA — Fri, 27 Jul 2012 07:11:48 GMT

←Older revision		Revision as of 07:11, 27 July 2012
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	[[Image:3gxe.png\|left\|200px]]		[[Image:3gxe.png\|left\|200px]]

-	<!--
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-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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	{{STRUCTURE_3gxe\| PDB=3gxe \| SCENE= }}		{{STRUCTURE_3gxe\| PDB=3gxe \| SCENE= }}

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	==About this Structure==		==About this Structure==
-	[[3gxe]] is a 4 chain structure of [[Fibronectin]] with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GXE OCA].	+	[[3gxe]] is a 4 chain structure of [[Collagen]] and [[Fibronectin]] with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GXE OCA].

	==See Also==		==See Also==
-	*[[Fibronectin]]	+	*[[Collagen\|Collagen]]
		+	*[[Fibronectin\|Fibronectin]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Campbell, I D.]]		[[Category: Campbell, I D.]]