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M409225200v1
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Papers In Press, published online ahead of print October 1, 2004
J. Biol. Chem, 10.1074/jbc.M409225200
Submitted on August 11, 2004
Revised on October 1, 2004
Accepted on October 1, 2004

Solution structure and dynamics of a prototypical chordin-like cysteine-rich repeat (VWC module) from collagen IIA

Joanne M. O'Leary, John M. Hamilton, Charlotte M. Deane, Najl V. Valeyev, Linda J. Sandell, and A. Kristina Downing

University of Oxford, Oxford, Oxon OX1 3QU

Corresponding Author: kristy{at}bioch.ox.ac.uk

Chordin-like cysteine-rich (CR) repeats (also referred to as 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 TGF-ß superfamily and are proposed to regulate growth factor signalling. Here we describe the intramolecular disulphide bonding, solution structure and dynamics of a prototypical chordinlike CR repeat from procollagen IIA (CRColIIA), which has been previously shown to bind TGF- ß1 and BMP-2. The CRColIIA 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 ß-sheet and the C-terminal region is more irregular with the fold constrained by disulphide bonds. Mobility between the N- and C-terminal sub-domains on a fast time scale 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 subdomain of the CR module and the fibronectin type 1 (FN1) 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 FN1 domains, we discuss the possibility that this structural homology might also have functional relevance.


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