Candidate cell and matrix interaction domains on the collagen fibril, the predominant protein of vertebrates.

ABSTRACT: Type I collagen, the predominant protein of vertebrates, polymerizes with type III and V collagens and non-collagenous molecules into large cable-like fibrils, yet how the fibril interacts with cells and other binding partners remains poorly understood. To help reveal insights into the collagen structure-function relationship, a data base was assembled including hundreds of type I collagen ligand binding sites and mutations on a two-dimensional model of the fibril. Visual examination of the distribution of functional sites, and statistical analysis of mutation distributions on the fibril suggest it is organized into two domains. The "cell interaction domain" is proposed to regulate dynamic aspects of collagen biology, including integrin-mediated cell interactions and fibril remodeling. The

SUBMITTER: Sweeney SM 

PROVIDER: S-EPMC2475701 | biostudies-literature | 2008 Jul

REPOSITORIES: biostudies-literature