3evs - Revision history

OCA at 00:25, 28 December 2023

OCA — Thu, 28 Dec 2023 00:25:00 GMT

←Older revision		Revision as of 00:25, 28 December 2023
Line 3:		Line 3:
	<StructureSection load='3evs' size='340' side='right'caption='[[3evs]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='3evs' size='340' side='right'caption='[[3evs]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3evs]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~] and [https://en.wikipedia.org/wiki/~~Lk3_transgenic_mice Lk3 transgenic mice~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EVS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EVS FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3evs]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EVS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EVS FirstGlance]. <br>
-	</td></tr><tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~><div style='overflow: auto; max-height: 3em;'>[[1rew\|1rew]], [[1waq\|1waq]], [[2k3g\|2k3g]], [[2qjb\|2qjb]], [[2h62\|2h62]]</div></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]] 2.1Å</td></tr>
-	~~<tr~~ id~~='gene'><td class~~="~~sblockLbl~~">~~<b>~~[[~~Gene~~\|~~Gene:~~]]~~</b></td><td class="sblockDat">CDMP1, GDF5 ([https://www~~.~~ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info~~&~~srchmode=5&id=9606 HUMAN]), Acvrlk6, Bmpr1b ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])~~</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=3evs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3evs OCA], [https://pdbe.org/3evs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3evs RCSB], [https://www.ebi.ac.uk/pdbsum/3evs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3evs 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=3evs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3evs OCA], [https://pdbe.org/3evs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3evs RCSB], [https://www.ebi.ac.uk/pdbsum/3evs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3evs ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/GDF5_HUMAN GDF5_HUMAN]] Defects in GDF5 are the cause of acromesomelic chondrodysplasia Grebe type (AMDG) [MIM:[https://omim.org/entry/200700 200700]]. Acromesomelic chondrodysplasias are rare hereditary skeletal disorders characterized by short stature, very short limbs, and hand/foot malformations. The severity of limb abnormalities increases from proximal to distal with profoundly affected hands and feet showing brachydactyly and/or rudimentary fingers (knob-like fingers). AMDG is an autosomal recessive form characterized by normal axial skeletons and missing or fused skeletal elements within the hands and feet.<ref>PMID:9288098</ref> Defects in GDF5 are the cause of acromesomelic chondrodysplasia Hunter-Thompson type (AMDH) [MIM:[https://omim.org/entry/201250 201250]]. AMDH is an autosomal recessive form of dwarfism. Patients have limb abnormalities, with the middle and distal segments being most affected and the lower limbs more affected than the upper. AMDH is characterized by normal axial skeletons and missing or fused skeletal elements within the hands and feet. Defects in GDF5 are the cause of brachydactyly type C (BDC) [MIM:[https://omim.org/entry/113100 113100]]. BDC is an autosomal dominant disorder characterized by an abnormal shortness of the fingers and toes. Note=Some BDC patients with GDF5 mutations also manifest clinical features of ASPED angel-shaped phalango-epiphyseal dysplasia (ASPED), an autosomal dominant skeletal abnormality characterized by a typical angel-shaped phalanx, brachydactyly, specific radiological findings, abnormal dentition, hip dysplasia, and delayed bone age. This suggests that BDC and ASPED are part of the same clinical spectrum (PubMed:22828468).<ref>PMID:22828468</ref> <ref>PMID:14735582</ref> Defects in GDF5 are the cause of Du Pan syndrome (DPS) [MIM:[https://omim.org/entry/228900 228900]]; also known as fibular hypoplasia and complex brachydactyly. Du Pan syndrome is a rare autosomal recessive condition characterized by absence of the fibulae and severe acromesomelic limb shortening with small, non-functional toes. Although milder, the phenotype resembles the autosomal recessive Hunter-Thompson and Grebe types of acromesomelic chondrodysplasia.<ref>PMID:12121354</ref> <ref>PMID:16222676</ref> <ref>PMID:18629880</ref> Defects in GDF5 are a cause of symphalangism proximal syndrome (SYM1) [MIM:[https://omim.org/entry/185800 185800]]. SYM1 is characterized by the hereditary absence of the proximal interphalangeal (PIP) joints (Cushing symphalangism). Severity of PIP joint involvement diminishes towards the radial side. Distal interphalangeal joints are less frequently involved and metacarpophalangeal joints are rarely affected whereas carpal bone malformation and fusion are common. In the lower extremities, tarsal bone coalition is common. Conducive hearing loss is seen and is due to fusion of the stapes to the petrous part of the temporal bone.<ref>PMID:16127465</ref> <ref>PMID:16892395</ref> <ref>PMID:18283415</ref> Defects in GDF5 are the cause of multiple synostoses syndrome type 2 (SYNS2) [MIM:[https://omim.org/entry/610017 610017]]. Multiple synostoses syndrome is an autosomal dominant condition characterized by progressive joint fusions of the fingers, wrists, ankles and cervical spine, characteristic facies and progressive conductive deafness.[:]<ref>PMID:16532400</ref> Defects in GDF5 are a cause of brachydactyly type A2 (BDA2) [MIM:[https://omim.org/entry/112600 112600]]. Brachydactylies (BDs) are a group of inherited malformations characterized by shortening of the digits due to abnormal development of the phalanges and/or the metacarpals. They have been classified on an anatomic and genetic basis into five groups, A to E, including three subgroups (A1 to A3) that usually manifest as autosomal dominant traits.<ref>PMID:16127465</ref> <ref>PMID:18203755</ref> Genetic variations in GDF5 are associated with susceptibility to osteoarthritis type 5 (OS5) [MIM:[https://omim.org/entry/612400 612400]]. Osteoarthritis is a degenerative disease of the joints characterized by degradation of the hyaline articular cartilage and remodeling of the subchondral bone with sclerosis. Clinical symptoms include pain and joint stiffness often leading to significant disability and joint replacement. Defects in GDF5 may be a cause of brachydactyly type A1 (BDA1) [MIM:[https://omim.org/entry/112500 112500]]. Brachydactylies (BDs) are a group of inherited malformations characterized by shortening of the digits due to abnormal development of the phalanges and/or the metacarpals. They have been classified on an anatomic and genetic basis into five groups, A to E, including three subgroups (A1 to A3) that usually manifest as autosomal dominant traits.<ref>PMID:20683927</ref>	+	[https://www.uniprot.org/uniprot/GDF5_HUMAN GDF5_HUMAN] Defects in GDF5 are the cause of acromesomelic chondrodysplasia Grebe type (AMDG) [MIM:[https://omim.org/entry/200700 200700]. Acromesomelic chondrodysplasias are rare hereditary skeletal disorders characterized by short stature, very short limbs, and hand/foot malformations. The severity of limb abnormalities increases from proximal to distal with profoundly affected hands and feet showing brachydactyly and/or rudimentary fingers (knob-like fingers). AMDG is an autosomal recessive form characterized by normal axial skeletons and missing or fused skeletal elements within the hands and feet.<ref>PMID:9288098</ref> Defects in GDF5 are the cause of acromesomelic chondrodysplasia Hunter-Thompson type (AMDH) [MIM:[https://omim.org/entry/201250 201250]. AMDH is an autosomal recessive form of dwarfism. Patients have limb abnormalities, with the middle and distal segments being most affected and the lower limbs more affected than the upper. AMDH is characterized by normal axial skeletons and missing or fused skeletal elements within the hands and feet. Defects in GDF5 are the cause of brachydactyly type C (BDC) [MIM:[https://omim.org/entry/113100 113100]. BDC is an autosomal dominant disorder characterized by an abnormal shortness of the fingers and toes. Note=Some BDC patients with GDF5 mutations also manifest clinical features of ASPED angel-shaped phalango-epiphyseal dysplasia (ASPED), an autosomal dominant skeletal abnormality characterized by a typical angel-shaped phalanx, brachydactyly, specific radiological findings, abnormal dentition, hip dysplasia, and delayed bone age. This suggests that BDC and ASPED are part of the same clinical spectrum (PubMed:22828468).<ref>PMID:22828468</ref> <ref>PMID:14735582</ref> Defects in GDF5 are the cause of Du Pan syndrome (DPS) [MIM:[https://omim.org/entry/228900 228900]; also known as fibular hypoplasia and complex brachydactyly. Du Pan syndrome is a rare autosomal recessive condition characterized by absence of the fibulae and severe acromesomelic limb shortening with small, non-functional toes. Although milder, the phenotype resembles the autosomal recessive Hunter-Thompson and Grebe types of acromesomelic chondrodysplasia.<ref>PMID:12121354</ref> <ref>PMID:16222676</ref> <ref>PMID:18629880</ref> Defects in GDF5 are a cause of symphalangism proximal syndrome (SYM1) [MIM:[https://omim.org/entry/185800 185800]. SYM1 is characterized by the hereditary absence of the proximal interphalangeal (PIP) joints (Cushing symphalangism). Severity of PIP joint involvement diminishes towards the radial side. Distal interphalangeal joints are less frequently involved and metacarpophalangeal joints are rarely affected whereas carpal bone malformation and fusion are common. In the lower extremities, tarsal bone coalition is common. Conducive hearing loss is seen and is due to fusion of the stapes to the petrous part of the temporal bone.<ref>PMID:16127465</ref> <ref>PMID:16892395</ref> <ref>PMID:18283415</ref> Defects in GDF5 are the cause of multiple synostoses syndrome type 2 (SYNS2) [MIM:[https://omim.org/entry/610017 610017]. Multiple synostoses syndrome is an autosomal dominant condition characterized by progressive joint fusions of the fingers, wrists, ankles and cervical spine, characteristic facies and progressive conductive deafness.[:]<ref>PMID:16532400</ref> Defects in GDF5 are a cause of brachydactyly type A2 (BDA2) [MIM:[https://omim.org/entry/112600 112600]. Brachydactylies (BDs) are a group of inherited malformations characterized by shortening of the digits due to abnormal development of the phalanges and/or the metacarpals. They have been classified on an anatomic and genetic basis into five groups, A to E, including three subgroups (A1 to A3) that usually manifest as autosomal dominant traits.<ref>PMID:16127465</ref> <ref>PMID:18203755</ref> Genetic variations in GDF5 are associated with susceptibility to osteoarthritis type 5 (OS5) [MIM:[https://omim.org/entry/612400 612400]. Osteoarthritis is a degenerative disease of the joints characterized by degradation of the hyaline articular cartilage and remodeling of the subchondral bone with sclerosis. Clinical symptoms include pain and joint stiffness often leading to significant disability and joint replacement. Defects in GDF5 may be a cause of brachydactyly type A1 (BDA1) [MIM:[https://omim.org/entry/112500 112500]. Brachydactylies (BDs) are a group of inherited malformations characterized by shortening of the digits due to abnormal development of the phalanges and/or the metacarpals. They have been classified on an anatomic and genetic basis into five groups, A to E, including three subgroups (A1 to A3) that usually manifest as autosomal dominant traits.<ref>PMID:20683927</ref>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/GDF5_HUMAN GDF5_HUMAN]] Could be involved in bone and cartilage formation. Chondrogenic signaling is mediated by the high-affinity receptor BMPR1B.<ref>PMID:15530414</ref> <ref>PMID:19229295</ref> [[https://www.uniprot.org/uniprot/BMR1B_MOUSE BMR1B_MOUSE]] On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for BMP7/OP-1 and GDF5.	+	[https://www.uniprot.org/uniprot/GDF5_HUMAN GDF5_HUMAN] Could be involved in bone and cartilage formation. Chondrogenic signaling is mediated by the high-affinity receptor BMPR1B.<ref>PMID:15530414</ref> <ref>PMID:19229295</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 39:		Line 38:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Lk3 transgenic mice~~]]	+	[[Category: Mus musculus]]
-	[[Category: Kotzsch, A]]	+	[[Category: Kotzsch A]]
-	[[Category: Mueller~~, T D]]~~	+	[[Category: Mueller TD]]
-	~~[[Category: Atp-binding]]~~	+
-	~~[[Category: Cleavage on pair of basic residue]]~~	+
-	~~[[Category: Cystin-knot ligand]]~~	+
-	~~[[Category: Cytokine]]~~	+
-	~~[[Category: Cytokine-transferase receptor complex]]~~	+
-	~~[[Category: Disease mutation]]~~	+
-	~~[[Category: Dwarfism]]~~	+
-	~~[[Category: Glycoprotein]]~~	+
-	~~[[Category: Growth factor]]~~	+
-	~~[[Category: Kinase]]~~	+
-	~~[[Category: Ligand-receptor complex]]~~	+
-	~~[[Category: Magnesium]]~~	+
-	~~[[Category: Manganese]]~~	+
-	~~[[Category: Membrane]]~~	+
-	~~[[Category: Metal-binding]]~~	+
-	~~[[Category: Nucleotide-binding]]~~	+
-	~~[[Category: Receptor]]~~	+
-	~~[[Category: Secreted]]~~	+
-	~~[[Category: Serine/threonine-protein kinase]]~~	+
-	~~[[Category: Transferase]]~~	+
-	~~[[Category: Transmembrane~~]]	+

OCA at 09:17, 23 February 2022

OCA — Wed, 23 Feb 2022 09:17:34 GMT

←Older revision		Revision as of 09:17, 23 February 2022
Line 1:		Line 1:

	==Crystal structure of the GDF-5:BMP receptor IB complex.==		==Crystal structure of the GDF-5:BMP receptor IB complex.==
-	<StructureSection load='3evs' size='340' side='right' caption='[[3evs]], [[Resolution\|resolution]] 2.10Å' scene=''>	+	<StructureSection load='3evs' size='340' side='right'caption='[[3evs]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3evs]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human] and [~~http~~://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EVS OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3EVS FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3evs]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human] and [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EVS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EVS FirstGlance]. <br>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1rew\|1rew]], [[1waq\|1waq]], [[2k3g\|2k3g]], [[2qjb\|2qjb]], [[2h62\|2h62]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1rew\|1rew]], [[1waq\|1waq]], [[2k3g\|2k3g]], [[2qjb\|2qjb]], [[2h62\|2h62]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CDMP1, GDF5 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), Acvrlk6, Bmpr1b ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CDMP1, GDF5 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), Acvrlk6, Bmpr1b ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=3evs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3evs OCA], [~~http~~://pdbe.org/3evs PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3evs RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3evs PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3evs 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=3evs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3evs OCA], [https://pdbe.org/3evs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3evs RCSB], [https://www.ebi.ac.uk/pdbsum/3evs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3evs ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/GDF5_HUMAN GDF5_HUMAN]] Defects in GDF5 are the cause of acromesomelic chondrodysplasia Grebe type (AMDG) [MIM:[~~http~~://omim.org/entry/200700 200700]]. Acromesomelic chondrodysplasias are rare hereditary skeletal disorders characterized by short stature, very short limbs, and hand/foot malformations. The severity of limb abnormalities increases from proximal to distal with profoundly affected hands and feet showing brachydactyly and/or rudimentary fingers (knob-like fingers). AMDG is an autosomal recessive form characterized by normal axial skeletons and missing or fused skeletal elements within the hands and feet.<ref>PMID:9288098</ref> Defects in GDF5 are the cause of acromesomelic chondrodysplasia Hunter-Thompson type (AMDH) [MIM:[~~http~~://omim.org/entry/201250 201250]]. AMDH is an autosomal recessive form of dwarfism. Patients have limb abnormalities, with the middle and distal segments being most affected and the lower limbs more affected than the upper. AMDH is characterized by normal axial skeletons and missing or fused skeletal elements within the hands and feet. Defects in GDF5 are the cause of brachydactyly type C (BDC) [MIM:[~~http~~://omim.org/entry/113100 113100]]. BDC is an autosomal dominant disorder characterized by an abnormal shortness of the fingers and toes. Note=Some BDC patients with GDF5 mutations also manifest clinical features of ASPED angel-shaped phalango-epiphyseal dysplasia (ASPED), an autosomal dominant skeletal abnormality characterized by a typical angel-shaped phalanx, brachydactyly, specific radiological findings, abnormal dentition, hip dysplasia, and delayed bone age. This suggests that BDC and ASPED are part of the same clinical spectrum (PubMed:22828468).<ref>PMID:22828468</ref> <ref>PMID:14735582</ref> Defects in GDF5 are the cause of Du Pan syndrome (DPS) [MIM:[~~http~~://omim.org/entry/228900 228900]]; also known as fibular hypoplasia and complex brachydactyly. Du Pan syndrome is a rare autosomal recessive condition characterized by absence of the fibulae and severe acromesomelic limb shortening with small, non-functional toes. Although milder, the phenotype resembles the autosomal recessive Hunter-Thompson and Grebe types of acromesomelic chondrodysplasia.<ref>PMID:12121354</ref> <ref>PMID:16222676</ref> <ref>PMID:18629880</ref> Defects in GDF5 are a cause of symphalangism proximal syndrome (SYM1) [MIM:[~~http~~://omim.org/entry/185800 185800]]. SYM1 is characterized by the hereditary absence of the proximal interphalangeal (PIP) joints (Cushing symphalangism). Severity of PIP joint involvement diminishes towards the radial side. Distal interphalangeal joints are less frequently involved and metacarpophalangeal joints are rarely affected whereas carpal bone malformation and fusion are common. In the lower extremities, tarsal bone coalition is common. Conducive hearing loss is seen and is due to fusion of the stapes to the petrous part of the temporal bone.<ref>PMID:16127465</ref> <ref>PMID:16892395</ref> <ref>PMID:18283415</ref> Defects in GDF5 are the cause of multiple synostoses syndrome type 2 (SYNS2) [MIM:[~~http~~://omim.org/entry/610017 610017]]. Multiple synostoses syndrome is an autosomal dominant condition characterized by progressive joint fusions of the fingers, wrists, ankles and cervical spine, characteristic facies and progressive conductive deafness.[:]<ref>PMID:16532400</ref> Defects in GDF5 are a cause of brachydactyly type A2 (BDA2) [MIM:[~~http~~://omim.org/entry/112600 112600]]. Brachydactylies (BDs) are a group of inherited malformations characterized by shortening of the digits due to abnormal development of the phalanges and/or the metacarpals. They have been classified on an anatomic and genetic basis into five groups, A to E, including three subgroups (A1 to A3) that usually manifest as autosomal dominant traits.<ref>PMID:16127465</ref> <ref>PMID:18203755</ref> Genetic variations in GDF5 are associated with susceptibility to osteoarthritis type 5 (OS5) [MIM:[~~http~~://omim.org/entry/612400 612400]]. Osteoarthritis is a degenerative disease of the joints characterized by degradation of the hyaline articular cartilage and remodeling of the subchondral bone with sclerosis. Clinical symptoms include pain and joint stiffness often leading to significant disability and joint replacement. Defects in GDF5 may be a cause of brachydactyly type A1 (BDA1) [MIM:[~~http~~://omim.org/entry/112500 112500]]. Brachydactylies (BDs) are a group of inherited malformations characterized by shortening of the digits due to abnormal development of the phalanges and/or the metacarpals. They have been classified on an anatomic and genetic basis into five groups, A to E, including three subgroups (A1 to A3) that usually manifest as autosomal dominant traits.<ref>PMID:20683927</ref>	+	[[https://www.uniprot.org/uniprot/GDF5_HUMAN GDF5_HUMAN]] Defects in GDF5 are the cause of acromesomelic chondrodysplasia Grebe type (AMDG) [MIM:[https://omim.org/entry/200700 200700]]. Acromesomelic chondrodysplasias are rare hereditary skeletal disorders characterized by short stature, very short limbs, and hand/foot malformations. The severity of limb abnormalities increases from proximal to distal with profoundly affected hands and feet showing brachydactyly and/or rudimentary fingers (knob-like fingers). AMDG is an autosomal recessive form characterized by normal axial skeletons and missing or fused skeletal elements within the hands and feet.<ref>PMID:9288098</ref> Defects in GDF5 are the cause of acromesomelic chondrodysplasia Hunter-Thompson type (AMDH) [MIM:[https://omim.org/entry/201250 201250]]. AMDH is an autosomal recessive form of dwarfism. Patients have limb abnormalities, with the middle and distal segments being most affected and the lower limbs more affected than the upper. AMDH is characterized by normal axial skeletons and missing or fused skeletal elements within the hands and feet. Defects in GDF5 are the cause of brachydactyly type C (BDC) [MIM:[https://omim.org/entry/113100 113100]]. BDC is an autosomal dominant disorder characterized by an abnormal shortness of the fingers and toes. Note=Some BDC patients with GDF5 mutations also manifest clinical features of ASPED angel-shaped phalango-epiphyseal dysplasia (ASPED), an autosomal dominant skeletal abnormality characterized by a typical angel-shaped phalanx, brachydactyly, specific radiological findings, abnormal dentition, hip dysplasia, and delayed bone age. This suggests that BDC and ASPED are part of the same clinical spectrum (PubMed:22828468).<ref>PMID:22828468</ref> <ref>PMID:14735582</ref> Defects in GDF5 are the cause of Du Pan syndrome (DPS) [MIM:[https://omim.org/entry/228900 228900]]; also known as fibular hypoplasia and complex brachydactyly. Du Pan syndrome is a rare autosomal recessive condition characterized by absence of the fibulae and severe acromesomelic limb shortening with small, non-functional toes. Although milder, the phenotype resembles the autosomal recessive Hunter-Thompson and Grebe types of acromesomelic chondrodysplasia.<ref>PMID:12121354</ref> <ref>PMID:16222676</ref> <ref>PMID:18629880</ref> Defects in GDF5 are a cause of symphalangism proximal syndrome (SYM1) [MIM:[https://omim.org/entry/185800 185800]]. SYM1 is characterized by the hereditary absence of the proximal interphalangeal (PIP) joints (Cushing symphalangism). Severity of PIP joint involvement diminishes towards the radial side. Distal interphalangeal joints are less frequently involved and metacarpophalangeal joints are rarely affected whereas carpal bone malformation and fusion are common. In the lower extremities, tarsal bone coalition is common. Conducive hearing loss is seen and is due to fusion of the stapes to the petrous part of the temporal bone.<ref>PMID:16127465</ref> <ref>PMID:16892395</ref> <ref>PMID:18283415</ref> Defects in GDF5 are the cause of multiple synostoses syndrome type 2 (SYNS2) [MIM:[https://omim.org/entry/610017 610017]]. Multiple synostoses syndrome is an autosomal dominant condition characterized by progressive joint fusions of the fingers, wrists, ankles and cervical spine, characteristic facies and progressive conductive deafness.[:]<ref>PMID:16532400</ref> Defects in GDF5 are a cause of brachydactyly type A2 (BDA2) [MIM:[https://omim.org/entry/112600 112600]]. Brachydactylies (BDs) are a group of inherited malformations characterized by shortening of the digits due to abnormal development of the phalanges and/or the metacarpals. They have been classified on an anatomic and genetic basis into five groups, A to E, including three subgroups (A1 to A3) that usually manifest as autosomal dominant traits.<ref>PMID:16127465</ref> <ref>PMID:18203755</ref> Genetic variations in GDF5 are associated with susceptibility to osteoarthritis type 5 (OS5) [MIM:[https://omim.org/entry/612400 612400]]. Osteoarthritis is a degenerative disease of the joints characterized by degradation of the hyaline articular cartilage and remodeling of the subchondral bone with sclerosis. Clinical symptoms include pain and joint stiffness often leading to significant disability and joint replacement. Defects in GDF5 may be a cause of brachydactyly type A1 (BDA1) [MIM:[https://omim.org/entry/112500 112500]]. Brachydactylies (BDs) are a group of inherited malformations characterized by shortening of the digits due to abnormal development of the phalanges and/or the metacarpals. They have been classified on an anatomic and genetic basis into five groups, A to E, including three subgroups (A1 to A3) that usually manifest as autosomal dominant traits.<ref>PMID:20683927</ref>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/GDF5_HUMAN GDF5_HUMAN]] Could be involved in bone and cartilage formation. Chondrogenic signaling is mediated by the high-affinity receptor BMPR1B.<ref>PMID:15530414</ref> <ref>PMID:19229295</ref> [[~~http~~://www.uniprot.org/uniprot/BMR1B_MOUSE BMR1B_MOUSE]] On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for BMP7/OP-1 and GDF5.	+	[[https://www.uniprot.org/uniprot/GDF5_HUMAN GDF5_HUMAN]] Could be involved in bone and cartilage formation. Chondrogenic signaling is mediated by the high-affinity receptor BMPR1B.<ref>PMID:15530414</ref> <ref>PMID:19229295</ref> [[https://www.uniprot.org/uniprot/BMR1B_MOUSE BMR1B_MOUSE]] On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for BMP7/OP-1 and GDF5.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 34:		Line 34:
	==See Also==		==See Also==
	*[[Growth differentiation factor\|Growth differentiation factor]]		*[[Growth differentiation factor\|Growth differentiation factor]]
		+	*[[Growth differentiation factor 3D STRUCTURES\|Growth differentiation factor 3D STRUCTURES]]
	== References ==		== References ==
	<references/>		<references/>
Line 39:		Line 40:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Lk3 transgenic mice]]		[[Category: Lk3 transgenic mice]]
	[[Category: Kotzsch, A]]		[[Category: Kotzsch, A]]

OCA at 21:19, 2 December 2018

OCA — Sun, 02 Dec 2018 21:19:43 GMT

←Older revision		Revision as of 21:19, 2 December 2018
Line 3:		Line 3:
	<StructureSection load='3evs' size='340' side='right' caption='[[3evs]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='3evs' size='340' side='right' caption='[[3evs]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3evs]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EVS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EVS FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3evs]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EVS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EVS FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1rew\|1rew]], [[1waq\|1waq]], [[2k3g\|2k3g]], [[2qjb\|2qjb]], [[2h62\|2h62]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1rew\|1rew]], [[1waq\|1waq]], [[2k3g\|2k3g]], [[2qjb\|2qjb]], [[2h62\|2h62]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Acvrlk6, Bmpr1b ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CDMP1, GDF5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), Acvrlk6, Bmpr1b ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=3evs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3evs OCA], [http://pdbe.org/3evs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3evs RCSB], [http://www.ebi.ac.uk/pdbsum/3evs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3evs 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=3evs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3evs OCA], [http://pdbe.org/3evs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3evs RCSB], [http://www.ebi.ac.uk/pdbsum/3evs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3evs ProSAT]</span></td></tr>
	</table>		</table>
Line 16:		Line 16:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ev/3evs_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ev/3evs_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>
Line 38:		Line 38:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Lk3 transgenic mice]]		[[Category: Lk3 transgenic mice]]
	[[Category: Kotzsch, A]]		[[Category: Kotzsch, A]]

OCA at 15:39, 5 August 2016

OCA — Fri, 05 Aug 2016 15:39:06 GMT

←Older revision		Revision as of 15:39, 5 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of the GDF-5:BMP receptor IB complex.==		==Crystal structure of the GDF-5:BMP receptor IB complex.==
	<StructureSection load='3evs' size='340' side='right' caption='[[3evs]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='3evs' size='340' side='right' caption='[[3evs]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3evs]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~] and [http://en.wikipedia.org/wiki/~~Mus_musculus Mus musculus~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EVS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EVS FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3evs]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EVS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EVS FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1rew\|1rew]], [[1waq\|1waq]], [[2k3g\|2k3g]], [[2qjb\|2qjb]], [[2h62\|2h62]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1rew\|1rew]], [[1waq\|1waq]], [[2k3g\|2k3g]], [[2qjb\|2qjb]], [[2h62\|2h62]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">~~CDMP1, GDF5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]),~~ Acvrlk6, Bmpr1b ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 ~~Mus musculus~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Acvrlk6, Bmpr1b ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=3evs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3evs OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3evs RCSB], [http://www.ebi.ac.uk/pdbsum/3evs 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=3evs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3evs OCA], [http://pdbe.org/3evs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3evs RCSB], [http://www.ebi.ac.uk/pdbsum/3evs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3evs ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 19:		Line 20:
	<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=3evs ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 29:		Line 30:
	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 3evs" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 36:		Line 38:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens]]~~	+	[[Category: Lk3 transgenic mice]]
-	~~[[Category: Mus musculus~~]]	+
	[[Category: Kotzsch, A]]		[[Category: Kotzsch, A]]
	[[Category: Mueller, T D]]		[[Category: Mueller, T D]]

OCA at 13:09, 18 December 2014

OCA — Thu, 18 Dec 2014 13:09:50 GMT

←Older revision		Revision as of 13:09, 18 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3evs\| PDB~~=3evs \| ~~SCENE~~= }}	+	==Crystal structure of the GDF-5:BMP receptor IB complex.==
-	===~~Crystal~~ structure of the ~~GDF~~-5:~~BMP~~ receptor IB complex.===	+	<StructureSection load='3evs' size='340' side='right' caption='[[3evs]], [[Resolution\|resolution]] 2.10Å' scene=''>
-	~~{{ABSTRACT_PUBMED_19229295}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3evs]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EVS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EVS FirstGlance]. <br>
		+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1rew\|1rew]], [[1waq\|1waq]], [[2k3g\|2k3g]], [[2qjb\|2qjb]], [[2h62\|2h62]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CDMP1, GDF5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), Acvrlk6, Bmpr1b ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</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=3evs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3evs OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3evs RCSB], [http://www.ebi.ac.uk/pdbsum/3evs PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/GDF5_HUMAN GDF5_HUMAN]] Defects in GDF5 are the cause of acromesomelic chondrodysplasia Grebe type (AMDG) [MIM:[http://omim.org/entry/200700 200700]]. Acromesomelic chondrodysplasias are rare hereditary skeletal disorders characterized by short stature, very short limbs, and hand/foot malformations. The severity of limb abnormalities increases from proximal to distal with profoundly affected hands and feet showing brachydactyly and/or rudimentary fingers (knob-like fingers). AMDG is an autosomal recessive form characterized by normal axial skeletons and missing or fused skeletal elements within the hands and feet.<ref>PMID:9288098</ref> Defects in GDF5 are the cause of acromesomelic chondrodysplasia Hunter-Thompson type (AMDH) [MIM:[http://omim.org/entry/201250 201250]]. AMDH is an autosomal recessive form of dwarfism. Patients have limb abnormalities, with the middle and distal segments being most affected and the lower limbs more affected than the upper. AMDH is characterized by normal axial skeletons and missing or fused skeletal elements within the hands and feet. Defects in GDF5 are the cause of brachydactyly type C (BDC) [MIM:[http://omim.org/entry/113100 113100]]. BDC is an autosomal dominant disorder characterized by an abnormal shortness of the fingers and toes. Note=Some BDC patients with GDF5 mutations also manifest clinical features of ASPED angel-shaped phalango-epiphyseal dysplasia (ASPED), an autosomal dominant skeletal abnormality characterized by a typical angel-shaped phalanx, brachydactyly, specific radiological findings, abnormal dentition, hip dysplasia, and delayed bone age. This suggests that BDC and ASPED are part of the same clinical spectrum (PubMed:22828468).<ref>PMID:22828468</ref> <ref>PMID:14735582</ref> Defects in GDF5 are the cause of Du Pan syndrome (DPS) [MIM:[http://omim.org/entry/228900 228900]]; also known as fibular hypoplasia and complex brachydactyly. Du Pan syndrome is a rare autosomal recessive condition characterized by absence of the fibulae and severe acromesomelic limb shortening with small, non-functional toes. Although milder, the phenotype resembles the autosomal recessive Hunter-Thompson and Grebe types of acromesomelic chondrodysplasia.<ref>PMID:12121354</ref> <ref>PMID:16222676</ref> <ref>PMID:18629880</ref> Defects in GDF5 are a cause of symphalangism proximal syndrome (SYM1) [MIM:[http://omim.org/entry/185800 185800]]. SYM1 is characterized by the hereditary absence of the proximal interphalangeal (PIP) joints (Cushing symphalangism). Severity of PIP joint involvement diminishes towards the radial side. Distal interphalangeal joints are less frequently involved and metacarpophalangeal joints are rarely affected whereas carpal bone malformation and fusion are common. In the lower extremities, tarsal bone coalition is common. Conducive hearing loss is seen and is due to fusion of the stapes to the petrous part of the temporal bone.<ref>PMID:16127465</ref> <ref>PMID:16892395</ref> <ref>PMID:18283415</ref> Defects in GDF5 are the cause of multiple synostoses syndrome type 2 (SYNS2) [MIM:[http://omim.org/entry/610017 610017]]. Multiple synostoses syndrome is an autosomal dominant condition characterized by progressive joint fusions of the fingers, wrists, ankles and cervical spine, characteristic facies and progressive conductive deafness.[:]<ref>PMID:16532400</ref> Defects in GDF5 are a cause of brachydactyly type A2 (BDA2) [MIM:[http://omim.org/entry/112600 112600]]. Brachydactylies (BDs) are a group of inherited malformations characterized by shortening of the digits due to abnormal development of the phalanges and/or the metacarpals. They have been classified on an anatomic and genetic basis into five groups, A to E, including three subgroups (A1 to A3) that usually manifest as autosomal dominant traits.<ref>PMID:16127465</ref> <ref>PMID:18203755</ref> Genetic variations in GDF5 are associated with susceptibility to osteoarthritis type 5 (OS5) [MIM:[http://omim.org/entry/612400 612400]]. Osteoarthritis is a degenerative disease of the joints characterized by degradation of the hyaline articular cartilage and remodeling of the subchondral bone with sclerosis. Clinical symptoms include pain and joint stiffness often leading to significant disability and joint replacement. Defects in GDF5 may be a cause of brachydactyly type A1 (BDA1) [MIM:[http://omim.org/entry/112500 112500]]. Brachydactylies (BDs) are a group of inherited malformations characterized by shortening of the digits due to abnormal development of the phalanges and/or the metacarpals. They have been classified on an anatomic and genetic basis into five groups, A to E, including three subgroups (A1 to A3) that usually manifest as autosomal dominant traits.<ref>PMID:20683927</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/GDF5_HUMAN GDF5_HUMAN]] Could be involved in bone and cartilage formation. Chondrogenic signaling is mediated by the high-affinity receptor BMPR1B.<ref>PMID:15530414</ref> <ref>PMID:19229295</ref> [[http://www.uniprot.org/uniprot/BMR1B_MOUSE BMR1B_MOUSE]] On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for BMP7/OP-1 and GDF5.
		+	== 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/ev/3evs_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 ==
		+	Dysregulation of growth and differentiation factor 5 (GDF-5) signalling, a member of the TGF-beta superfamily, is strongly linked to skeletal malformation. GDF-5-mediated signal transduction involves both BMP type I receptors, BMPR-IA and BMPR-IB. However, mutations in either GDF-5 or BMPR-IB lead to similar phenotypes, indicating that in chondrogenesis GDF-5 signalling seems to be exclusively mediated through BMPR-IB. Here, we present structural insights into the GDF-5:BMPR-IB complex revealing how binding specificity for BMPR-IB is generated on a molecular level. In BMPR-IB, a loop within the ligand-binding epitope functions similar to a latch allowing high-affinity binding of GDF-5. In BMPR-IA, this latch is in a closed conformation leading to steric repulsion. The new structural data now provide also a molecular basis of how phenotypically relevant missense mutations in GDF-5 might impair receptor binding and activation.

-	~~==Disease==~~	+	Crystal structure analysis reveals a spring-loaded latch as molecular mechanism for GDF-5-type I receptor specificity.,Kotzsch A, Nickel J, Seher A, Sebald W, Muller TD EMBO J. 2009 Apr 8;28(7):937-47. Epub 2009 Feb 19. PMID:19229295<ref>PMID:19229295</ref>
-	[[http://www.uniprot.org/uniprot/GDF5_HUMAN GDF5_HUMAN]] Defects in GDF5 are the cause of acromesomelic chondrodysplasia Grebe type (AMDG) [MIM:[http://omim.org/entry/200700 200700]]. Acromesomelic chondrodysplasias are rare hereditary skeletal disorders characterized by short stature, very short limbs, and hand/foot malformations. The severity of limb abnormalities increases from proximal to distal with profoundly affected hands and feet showing brachydactyly and/or rudimentary fingers (knob-like fingers). AMDG is an autosomal recessive form characterized by normal axial skeletons and missing or fused skeletal elements within the hands and feet.<ref>PMID:9288098</ref> Defects in GDF5 are the cause of acromesomelic chondrodysplasia Hunter-Thompson type (AMDH) [MIM:[http://omim.org/entry/201250 201250]]. AMDH is an autosomal recessive form of dwarfism. Patients have limb abnormalities, with the middle and distal segments being most affected and the lower limbs more affected than the upper. AMDH is characterized by normal axial skeletons and missing or fused skeletal elements within the hands and feet. Defects in GDF5 are the cause of brachydactyly type C (BDC) [MIM:[http://omim.org/entry/113100 113100]]. BDC is an autosomal dominant disorder characterized by an abnormal shortness of the fingers and toes. Note=Some BDC patients with GDF5 mutations also manifest clinical features of ASPED angel-shaped phalango-epiphyseal dysplasia (ASPED), an autosomal dominant skeletal abnormality characterized by a ~~typical angel~~-shaped phalanx, brachydactyly, specific radiological findings, abnormal dentition, hip dysplasia, and delayed bone age. This suggests that BDC and ASPED are part of the same clinical spectrum (PubMed:22828468).<ref>PMID:22828468</ref><ref>PMID:14735582</ref> Defects in GDF5 are the cause of Du Pan syndrome (DPS) [MIM:[http://omim.org/entry/228900 228900]]; also known as ~~fibular hypoplasia and complex brachydactyly. Du Pan syndrome is a rare autosomal recessive condition characterized by absence of the fibulae and severe acromesomelic limb shortening with small, non~~-~~functional toes. Although milder, the phenotype resembles the autosomal recessive Hunter~~-Thompson and Grebe types of acromesomelic chondrodysplasia.<ref>PMID:12121354</ref><ref>PMID:16222676</ref><ref>PMID:18629880</ref> Defects in GDF5 are a cause of symphalangism proximal syndrome (SYM1) [MIM:[http://omim.org/entry/185800 185800]]. SYM1 is characterized by the hereditary absence of the proximal interphalangeal (PIP) joints (Cushing symphalangism). Severity of PIP joint involvement diminishes towards the radial side. Distal interphalangeal joints are less frequently involved and metacarpophalangeal joints are rarely affected whereas carpal bone malformation and fusion are common. In the lower extremities, tarsal bone coalition is common. Conducive hearing loss is seen and is due to fusion of the stapes to the petrous part of the temporal bone.<ref>PMID:16127465</ref><ref>PMID:16892395</ref><ref>PMID:18283415</ref> Defects in GDF5 are the cause of multiple synostoses syndrome type ~~2 (SYNS2) [MIM:[http://omim~~.~~org/entry/610017 610017]]. Multiple synostoses syndrome is an autosomal dominant condition characterized by progressive joint fusions of the fingers~~, ~~wrists~~, ankles and cervical spine, characteristic facies and progressive conductive deafness.[:]<ref>PMID:16532400</ref> Defects in GDF5 are a cause of brachydactyly type A2 (BDA2) [MIM:[http://omim.org/entry/112600 112600]]. Brachydactylies (BDs) are a group of inherited malformations characterized by shortening of the digits due to abnormal development of the phalanges and/or the metacarpals. They have been classified on an anatomic and genetic basis into five groups, A ~~to E~~, ~~including three subgroups (A1 to A3) that usually manifest as autosomal dominant traits~~.~~<ref>PMID:16127465</ref><ref>PMID:18203755</ref> Genetic variations in GDF5 are associated with susceptibility to osteoarthritis type 5~~ (~~OS5~~) ~~[MIM~~:~~[http://omim~~.~~org/entry/612400 612400]]~~. Osteoarthritis is a degenerative disease of the joints characterized by degradation of the hyaline articular cartilage and remodeling of the subchondral bone with sclerosis. Clinical symptoms include pain and joint stiffness often leading to significant disability and joint replacement. Defects in GDF5 may be a cause of brachydactyly type A1 (BDA1) [MIM:[http://omim.org/entry/112500 112500]]. Brachydactylies (BDs) are a group of inherited malformations characterized by shortening of the digits due to abnormal development of the phalanges and/or the metacarpals. They have been classified on an anatomic and genetic basis into five groups, A to E, including three subgroups (A1 to A3) that usually manifest as autosomal dominant traits.<ref>PMID:~~20683927~~</ref>	+

-	~~==Function==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[http:~~/~~/www~~.~~uniprot~~.~~org/uniprot/GDF5_HUMAN GDF5_HUMAN]] Could be involved in bone and cartilage formation. Chondrogenic signaling is mediated by the high-affinity receptor BMPR1B~~.<~~ref~~>~~PMID:15530414~~</~~ref~~><ref>PMID:19229295</ref> [[http://www.uniprot.org/uniprot/BMR1B_MOUSE BMR1B_MOUSE]] On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for BMP7/OP-1 and GDF5.	+	</div>

-	==~~About this Structure~~==	+	==See Also==
-	[[~~3evs~~]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EVS OCA].	+	*[[Growth differentiation factor\|Growth differentiation factor]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:019229295</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Mus musculus]]		[[Category: Mus musculus]]
-	[[Category: Kotzsch, A.]]	+	[[Category: Kotzsch, A]]
-	[[Category: Mueller, T D.]]	+	[[Category: Mueller, T D]]
	[[Category: Atp-binding]]		[[Category: Atp-binding]]
	[[Category: Cleavage on pair of basic residue]]		[[Category: Cleavage on pair of basic residue]]

OCA at 00:56, 25 March 2013

OCA — Mon, 25 Mar 2013 00:56:19 GMT

←Older revision		Revision as of 00:56, 25 March 2013
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-	[[Image:3evs.png\|left\|200px]]
-
	{{STRUCTURE_3evs\| PDB=3evs \| SCENE= }}		{{STRUCTURE_3evs\| PDB=3evs \| SCENE= }}
-
	===Crystal structure of the GDF-5:BMP receptor IB complex.===		===Crystal structure of the GDF-5:BMP receptor IB complex.===
		+	{{ABSTRACT_PUBMED_19229295}}

-	~~{{ABSTRACT_PUBMED_19229295}}~~	+	==Disease==
		+	[[http://www.uniprot.org/uniprot/GDF5_HUMAN GDF5_HUMAN]] Defects in GDF5 are the cause of acromesomelic chondrodysplasia Grebe type (AMDG) [MIM:[http://omim.org/entry/200700 200700]]. Acromesomelic chondrodysplasias are rare hereditary skeletal disorders characterized by short stature, very short limbs, and hand/foot malformations. The severity of limb abnormalities increases from proximal to distal with profoundly affected hands and feet showing brachydactyly and/or rudimentary fingers (knob-like fingers). AMDG is an autosomal recessive form characterized by normal axial skeletons and missing or fused skeletal elements within the hands and feet.<ref>PMID:9288098</ref> Defects in GDF5 are the cause of acromesomelic chondrodysplasia Hunter-Thompson type (AMDH) [MIM:[http://omim.org/entry/201250 201250]]. AMDH is an autosomal recessive form of dwarfism. Patients have limb abnormalities, with the middle and distal segments being most affected and the lower limbs more affected than the upper. AMDH is characterized by normal axial skeletons and missing or fused skeletal elements within the hands and feet. Defects in GDF5 are the cause of brachydactyly type C (BDC) [MIM:[http://omim.org/entry/113100 113100]]. BDC is an autosomal dominant disorder characterized by an abnormal shortness of the fingers and toes. Note=Some BDC patients with GDF5 mutations also manifest clinical features of ASPED angel-shaped phalango-epiphyseal dysplasia (ASPED), an autosomal dominant skeletal abnormality characterized by a typical angel-shaped phalanx, brachydactyly, specific radiological findings, abnormal dentition, hip dysplasia, and delayed bone age. This suggests that BDC and ASPED are part of the same clinical spectrum (PubMed:22828468).<ref>PMID:22828468</ref><ref>PMID:14735582</ref> Defects in GDF5 are the cause of Du Pan syndrome (DPS) [MIM:[http://omim.org/entry/228900 228900]]; also known as fibular hypoplasia and complex brachydactyly. Du Pan syndrome is a rare autosomal recessive condition characterized by absence of the fibulae and severe acromesomelic limb shortening with small, non-functional toes. Although milder, the phenotype resembles the autosomal recessive Hunter-Thompson and Grebe types of acromesomelic chondrodysplasia.<ref>PMID:12121354</ref><ref>PMID:16222676</ref><ref>PMID:18629880</ref> Defects in GDF5 are a cause of symphalangism proximal syndrome (SYM1) [MIM:[http://omim.org/entry/185800 185800]]. SYM1 is characterized by the hereditary absence of the proximal interphalangeal (PIP) joints (Cushing symphalangism). Severity of PIP joint involvement diminishes towards the radial side. Distal interphalangeal joints are less frequently involved and metacarpophalangeal joints are rarely affected whereas carpal bone malformation and fusion are common. In the lower extremities, tarsal bone coalition is common. Conducive hearing loss is seen and is due to fusion of the stapes to the petrous part of the temporal bone.<ref>PMID:16127465</ref><ref>PMID:16892395</ref><ref>PMID:18283415</ref> Defects in GDF5 are the cause of multiple synostoses syndrome type 2 (SYNS2) [MIM:[http://omim.org/entry/610017 610017]]. Multiple synostoses syndrome is an autosomal dominant condition characterized by progressive joint fusions of the fingers, wrists, ankles and cervical spine, characteristic facies and progressive conductive deafness.[:]<ref>PMID:16532400</ref> Defects in GDF5 are a cause of brachydactyly type A2 (BDA2) [MIM:[http://omim.org/entry/112600 112600]]. Brachydactylies (BDs) are a group of inherited malformations characterized by shortening of the digits due to abnormal development of the phalanges and/or the metacarpals. They have been classified on an anatomic and genetic basis into five groups, A to E, including three subgroups (A1 to A3) that usually manifest as autosomal dominant traits.<ref>PMID:16127465</ref><ref>PMID:18203755</ref> Genetic variations in GDF5 are associated with susceptibility to osteoarthritis type 5 (OS5) [MIM:[http://omim.org/entry/612400 612400]]. Osteoarthritis is a degenerative disease of the joints characterized by degradation of the hyaline articular cartilage and remodeling of the subchondral bone with sclerosis. Clinical symptoms include pain and joint stiffness often leading to significant disability and joint replacement. Defects in GDF5 may be a cause of brachydactyly type A1 (BDA1) [MIM:[http://omim.org/entry/112500 112500]]. Brachydactylies (BDs) are a group of inherited malformations characterized by shortening of the digits due to abnormal development of the phalanges and/or the metacarpals. They have been classified on an anatomic and genetic basis into five groups, A to E, including three subgroups (A1 to A3) that usually manifest as autosomal dominant traits.<ref>PMID:20683927</ref>
		+
		+	==Function==
		+	[[http://www.uniprot.org/uniprot/GDF5_HUMAN GDF5_HUMAN]] Could be involved in bone and cartilage formation. Chondrogenic signaling is mediated by the high-affinity receptor BMPR1B.<ref>PMID:15530414</ref><ref>PMID:19229295</ref> [[http://www.uniprot.org/uniprot/BMR1B_MOUSE BMR1B_MOUSE]] On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for BMP7/OP-1 and GDF5.

	==About this Structure==		==About this Structure==
Line 11:		Line 13:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:019229295</ref><references group="xtra"/>	+	<ref group="xtra">PMID:019229295</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Mus musculus]]		[[Category: Mus musculus]]

OCA: Protected "3evs" [edit=sysop:move=sysop]

OCA — Wed, 06 Feb 2013 13:16:54 GMT

Protected "3evs" [edit=sysop:move=sysop]

←Older revision

Revision as of 13:16, 6 February 2013

OCA at 13:16, 6 February 2013

OCA — Wed, 06 Feb 2013 13:16:50 GMT

←Older revision		Revision as of 13:16, 6 February 2013
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-	{{Seed}}
	[[Image:3evs.png\|left\|200px]]		[[Image:3evs.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_3evs", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
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-	-->
	{{STRUCTURE_3evs\| PDB=3evs \| SCENE= }}		{{STRUCTURE_3evs\| PDB=3evs \| SCENE= }}

	===Crystal structure of the GDF-5:BMP receptor IB complex.===		===Crystal structure of the GDF-5:BMP receptor IB complex.===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_19229295}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 19229295 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_19229295}}		{{ABSTRACT_PUBMED_19229295}}

	==About this Structure==		==About this Structure==
-	~~3EVS~~ is a 2 ~~chains~~ structure ~~of sequences~~ from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EVS OCA].	+	[[3evs]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EVS OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~19229295~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:019229295</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Mus musculus]]		[[Category: Mus musculus]]
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	[[Category: Cystin-knot ligand]]		[[Category: Cystin-knot ligand]]
	[[Category: Cytokine]]		[[Category: Cytokine]]
-	[[Category: Cytokine/transferase receptor complex]]	+	[[Category: Cytokine-transferase receptor complex]]
	[[Category: Disease mutation]]		[[Category: Disease mutation]]
	[[Category: Dwarfism]]		[[Category: Dwarfism]]
Line 44:		Line 32:
	[[Category: Metal-binding]]		[[Category: Metal-binding]]
	[[Category: Nucleotide-binding]]		[[Category: Nucleotide-binding]]
-	[[Category: Polymorphism]]
	[[Category: Receptor]]		[[Category: Receptor]]
	[[Category: Secreted]]		[[Category: Secreted]]
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	[[Category: Transferase]]		[[Category: Transferase]]
	[[Category: Transmembrane]]		[[Category: Transmembrane]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 10 18:51:54 2009''

OCA at 15:51, 10 June 2009

OCA — Wed, 10 Jun 2009 15:51:56 GMT

←Older revision		Revision as of 15:51, 10 June 2009
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	{{Seed}}		{{Seed}}
-	[[Image:3evs.~~jpg~~\|left\|200px]]	+	[[Image:3evs.png\|left\|200px]]

	<!--		<!--
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-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed ~~Mar 11 11~~:15:21 2009''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 10 18:51:54 2009''

OCA at 09:15, 11 March 2009

OCA — Wed, 11 Mar 2009 09:15:22 GMT

←Older revision		Revision as of 09:15, 11 March 2009
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-	~~'''Unreleased structure'''~~	+	{{Seed}}
		+	[[Image:3evs.jpg\|left\|200px]]

-	The ~~entry 3evs~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3evs", creates the "Structure Box" on the page.
		+	You may change the PDB parameter (which sets the PDB file loaded into the applet)
		+	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
		+	or leave the SCENE parameter empty for the default display.
		+	-->
		+	{{STRUCTURE_3evs\| PDB=3evs \| SCENE= }}

-	~~Authors~~: ~~Kotzsch, A., Mueller, T.D~~.	+	===Crystal structure of the GDF-5:BMP receptor IB complex.===

-	Description: Crystal structure of the GDF-5:BMP receptor IB complex.

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed ~~Oct 29 10~~:29:~~26 2008~~''	+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_19229295}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 19229295 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_19229295}}
		+
		+	==About this Structure==
		+	3EVS is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EVS OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:19229295</ref><references group="xtra"/>
		+	[[Category: Homo sapiens]]
		+	[[Category: Mus musculus]]
		+	[[Category: Kotzsch, A.]]
		+	[[Category: Mueller, T D.]]
		+	[[Category: Atp-binding]]
		+	[[Category: Cleavage on pair of basic residue]]
		+	[[Category: Cystin-knot ligand]]
		+	[[Category: Cytokine]]
		+	[[Category: Cytokine/transferase receptor complex]]
		+	[[Category: Disease mutation]]
		+	[[Category: Dwarfism]]
		+	[[Category: Glycoprotein]]
		+	[[Category: Growth factor]]
		+	[[Category: Kinase]]
		+	[[Category: Ligand-receptor complex]]
		+	[[Category: Magnesium]]
		+	[[Category: Manganese]]
		+	[[Category: Membrane]]
		+	[[Category: Metal-binding]]
		+	[[Category: Nucleotide-binding]]
		+	[[Category: Polymorphism]]
		+	[[Category: Receptor]]
		+	[[Category: Secreted]]
		+	[[Category: Serine/threonine-protein kinase]]
		+	[[Category: Transferase]]
		+	[[Category: Transmembrane]]
		+
		+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 11 11:15:21 2009''