1o91

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spinqualitylabelsall models 1o91, resolution 1.9Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF A COLLAGEN VIII NC1 DOMAIN TRIMER

Overview

Collagen VIII is a major component of Descemet's membrane and is also, found in vascular subendothelial matrices. The C-terminal non-collagenous, domain (NC1) domain of collagen VIII, which is a member of the C1q-like, protein family, forms a stable trimer and is thought to direct the, assembly of the collagen triple helix, as well as polygonal supramolecular, structures. We have solved the crystal structure of the mouse, alpha1(VIII)(3) NC1 domain trimer at 1.9 A resolution. Each subunit of the, intimate NC1 trimer consists of a ten-stranded beta-sandwich. The surface, of the collagen VIII NC1 trimer presents three strips of partially exposed, aromatic residues shown to interact with the non-ionic detergent CHAPS, which are likely to be involved in supramolecular assemblies. Equivalent, strips exist in the NC1 domain of the closely related collagen X, suggesting a conserved assembly mechanism. Surprisingly, the collagen VIII, NC1 trimer lacks the buried calcium cluster of the collagen X NC1 trimer., The mouse alpha1(VIII) and alpha2(VIII) NC1 domains are 71.5% identical in, sequence, with the differences being concentrated on the NC1 trimer, surface. A few non-conservative substitutions map to the subunit, interfaces near the surface, but it is not obvious from the structure to, what extent they determine the preferred assembly of collagen VIII alpha1, and alpha2 chains into homotrimers.

About this Structure

1O91 is a Single protein structure of sequence from Mus musculus with SO4 and CPS as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

Crystal structure of the collagen alpha1(VIII) NC1 trimer., Kvansakul M, Bogin O, Hohenester E, Yayon A, Matrix Biol. 2003 Apr;22(2):145-52. PMID:12782141

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