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| [[Image:1u5m.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1u5m| PDB=1u5m | SCENE= }} | | {{STRUCTURE_1u5m| PDB=1u5m | SCENE= }} |
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| '''Structure of a Chordin-like Cysteine-rich Repeat (VWC module) from Collagen IIA'''
| | ===Structure of a Chordin-like Cysteine-rich Repeat (VWC module) from Collagen IIA=== |
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| ==Overview==
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| Chordin-like cysteine-rich (CR) repeats (also referred to as von Willebrand factor type C (VWC) modules) have been identified in approximately 200 extracellular matrix proteins. These repeats, named on the basis of amino acid conservation of 10 cysteine residues, have been shown to bind members of the transforming growth factor-beta (TGF-beta) superfamily and are proposed to regulate growth factor signaling. Here we describe the intramolecular disulfide bonding, solution structure, and dynamics of a prototypical chordin-like CR repeat from procollagen IIA (CR(ColIIA)), which has been previously shown to bind TGF-beta1 and bone morphogenetic protein-2. The CR(ColIIA) structure manifests a two sub-domain architecture tethered by a flexible linkage. Initial structures were calculated using RosettaNMR, a de novo prediction method, and final structure calculations were performed using CANDID within CYANA. The N-terminal region contains mainly beta-sheet and the C-terminal region is more irregular with the fold constrained by disulfide bonds. Mobility between the N- and C-terminal sub-domains on a fast timescale was confirmed using NMR relaxation measurements. We speculate that the mobility between the two sub-domains may decrease upon ligand binding. Structure and sequence comparisons have revealed an evolutionary relationship between the N-terminal sub-domain of the CR module and the fibronectin type 1 domain, suggesting that these domains share a common ancestry. Based on the previously reported mapping of fibronectin binding sites for vascular endothelial growth factor to regions containing fibronectin type 1 domains, we discuss the possibility that this structural homology might also have functional relevance.
| | The line below this paragraph, {{ABSTRACT_PUBMED_15466413}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15466413 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15466413}} |
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| ==Disease== | | ==Disease== |
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| ==About this Structure== | | ==About this Structure== |
| 1U5M is a [[Single protein]] structure of 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=1U5M OCA]. | | 1U5M is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U5M OCA]. |
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| ==Reference== | | ==Reference== |
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| [[Category: Beta-sheet]] | | [[Category: Beta-sheet]] |
| [[Category: Two sub-domain architecture]] | | [[Category: Two sub-domain architecture]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:47:07 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 12:52:19 2008'' |
