5dft - Revision history

OCA at 12:24, 6 March 2024

2024-03-06T12:24:22Z

←Older revision		Revision as of 12:24, 6 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5dft]] is a 10 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=5DFT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DFT FirstGlance]. <br>		<table><tr><td colspan='2'>[[5dft]] is a 10 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=5DFT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DFT FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</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]] 2.5Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene></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=5dft FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dft OCA], [https://pdbe.org/5dft PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dft RCSB], [https://www.ebi.ac.uk/pdbsum/5dft PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dft 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=5dft FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dft OCA], [https://pdbe.org/5dft PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dft RCSB], [https://www.ebi.ac.uk/pdbsum/5dft PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dft ProSAT]</span></td></tr>
	</table>		</table>

OCA at 10:33, 21 June 2023

2023-06-21T10:33:33Z

←Older revision		Revision as of 10:33, 21 June 2023
Line 3:		Line 3:
	<StructureSection load='5dft' size='340' side='right'caption='[[5dft]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='5dft' size='340' side='right'caption='[[5dft]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5dft]] is a 10 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=5DFT OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5DFT FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5dft]] is a 10 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=5DFT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DFT FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FN1, 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'>[https://proteopedia.org/fgij/fg.htm?mol=5dft FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dft OCA], [https://pdbe.org/5dft PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dft RCSB], [https://www.ebi.ac.uk/pdbsum/5dft PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dft ProSAT]</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=5dft FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dft OCA], [~~http~~://pdbe.org/5dft PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5dft RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5dft PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5dft 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>	+	[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 ==
-	[~~[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>	+	[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>

	==See Also==		==See Also==
Line 19:		Line 18:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Briknarova, K]]	+	[[Category: Briknarova K]]
-	[[Category: Mou~~, T C~~]]	+	[[Category: Mou TC]]
-	[[Category: Rusnac, D V]]	+	[[Category: Rusnac D-V]]
-	[[Category: Sprang~~, S R]]~~	+	[[Category: Sprang SR]]
-	~~[[Category: Cell adhesion]]~~	+
-	~~[[Category: Fibronectin]]~~	+
-	~~[[Category: Fn3 domain~~]]	+

OCA at 07:31, 27 November 2019

2019-11-27T07:31:20Z

←Older revision		Revision as of 07:31, 27 November 2019
Line 1:		Line 1:

	==Structure of the Eleventh Type III Domain from Human Fibronectin==		==Structure of the Eleventh Type III Domain from Human Fibronectin==
-	<StructureSection load='5dft' size='340' side='right' caption='[[5dft]], [[Resolution\|resolution]] 2.50Å' scene=''>	+	<StructureSection load='5dft' size='340' side='right'caption='[[5dft]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5dft]] is a 10 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=5DFT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DFT FirstGlance]. <br>		<table><tr><td colspan='2'>[[5dft]] is a 10 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=5DFT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DFT FirstGlance]. <br>
Line 12:		Line 12:
	== 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/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>
		+
		+	==See Also==
		+	*[[Fibronectin 3D structures\|Fibronectin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 17:		Line 20:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Briknarova, K]]		[[Category: Briknarova, K]]
	[[Category: Mou, T C]]		[[Category: Mou, T C]]

OCA at 16:51, 15 November 2017

2017-11-15T16:51:13Z

←Older revision		Revision as of 16:51, 15 November 2017
Line 3:		Line 3:
	<StructureSection load='5dft' size='340' side='right' caption='[[5dft]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='5dft' size='340' side='right' caption='[[5dft]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5dft]] is a 10 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DFT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DFT FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5dft]] is a 10 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=5DFT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DFT FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FN1, 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=5dft FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dft OCA], [http://pdbe.org/5dft PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dft RCSB], [http://www.ebi.ac.uk/pdbsum/5dft PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5dft ProSAT]</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=5dft FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dft OCA], [http://pdbe.org/5dft PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dft RCSB], [http://www.ebi.ac.uk/pdbsum/5dft PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5dft ProSAT]</span></td></tr>
	</table>		</table>
Line 15:		Line 16:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Briknarova, K]]		[[Category: Briknarova, K]]
	[[Category: Mou, T C]]		[[Category: Mou, T C]]

OCA at 15:28, 14 September 2016

2016-09-14T15:28:24Z

←Older revision		Revision as of 15:28, 14 September 2016
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5dft is ~~ON HOLD until Paper Publication~~	+	==Structure of the Eleventh Type III Domain from Human Fibronectin==
-		+	<StructureSection load='5dft' size='340' side='right' caption='[[5dft]], [[Resolution\|resolution]] 2.50Å' scene=''>
-	~~Authors~~: ~~Rusnac, D~~.-V., ~~Mou, T~~.C., ~~Sprang~~, S.R., ~~Briknarova~~, K.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5dft]] is a 10 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DFT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DFT FirstGlance]. <br>
-	~~Description~~: ~~Structure~~ of the ~~Eleventh Type III Domain from Human Fibronectin~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene></td></tr>
-	[[~~Category~~: ~~Unreleased Structures~~]]	+	<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=5dft FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dft OCA], [http://pdbe.org/5dft PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dft RCSB], [http://www.ebi.ac.uk/pdbsum/5dft PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5dft ProSAT]</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>
		+	== 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>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Briknarova, K]]		[[Category: Briknarova, K]]
-	[[Category: ~~Rusnac~~, ~~D.-V~~]]	+	[[Category: Mou, T C]]
-	[[Category: ~~Mou~~, ~~T.C~~]]	+	[[Category: Rusnac, D V]]
-	[[Category: Sprang, S.R]]	+	[[Category: Sprang, S R]]
		+	[[Category: Cell adhesion]]
		+	[[Category: Fibronectin]]
		+	[[Category: Fn3 domain]]

OCA at 11:07, 16 December 2015

2015-12-16T11:07:40Z

←Older revision		Revision as of 11:07, 16 December 2015
Line 7:		Line 7:
	Description: Structure of the Eleventh Type III Domain from Human Fibronectin		Description: Structure of the Eleventh Type III Domain from Human Fibronectin
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
-	[[Category: Mou, T.C]]
	[[Category: Briknarova, K]]		[[Category: Briknarova, K]]
	[[Category: Rusnac, D.-V]]		[[Category: Rusnac, D.-V]]
		+	[[Category: Mou, T.C]]
	[[Category: Sprang, S.R]]		[[Category: Sprang, S.R]]

OCA at 02:19, 16 October 2015

2015-10-16T02:19:43Z

←Older revision		Revision as of 02:19, 16 October 2015
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5dft is ON HOLD	+	The entry 5dft is ON HOLD until Paper Publication

	Authors: Rusnac, D.-V., Mou, T.C., Sprang, S.R., Briknarova, K.		Authors: Rusnac, D.-V., Mou, T.C., Sprang, S.R., Briknarova, K.

OCA: Protected "5dft" [edit=sysop:move=sysop]

2015-09-02T11:35:56Z

Protected "5dft" [edit=sysop:move=sysop]

←Older revision

Revision as of 11:35, 2 September 2015

OCA: New page: '''Unreleased structure''' The entry 5dft is ON HOLD Authors: Rusnac, D.-V., Mou, T.C., Sprang, S.R., Briknarova, K. Description: Structure of the Eleventh Type III Domain from Human F...

2015-09-02T11:35:54Z

New page: '''Unreleased structure''' The entry 5dft is ON HOLD Authors: Rusnac, D.-V., Mou, T.C., Sprang, S.R., Briknarova, K. Description: Structure of the Eleventh Type III Domain from Human F...

New page

'''Unreleased structure'''

The entry 5dft is ON HOLD

Authors: Rusnac, D.-V., Mou, T.C., Sprang, S.R., Briknarova, K.

Description: Structure of the Eleventh Type III Domain from Human Fibronectin
[[Category: Unreleased Structures]]
[[Category: Mou, T.C]]
[[Category: Briknarova, K]]
[[Category: Rusnac, D.-V]]
[[Category: Sprang, S.R]]