The modular architecture of vertebrate collagens

FEBS Letters

Bork, Peer¹ 

[1] EMBL, Meyerhofstr. 1, 6900 Heidelberg, and Max-Delbrück-Centre for Molecular Medicine, Robert-Rössle-Str. 10, 1115 Berlin, Germany

关键词: Homology;    Mosaic protein;    Type VII collagen;    Thrombospondin;    NC;    noncollagenous;    Fn3;    fibronectin type III;    VWA;    von Willebrand factor type A;    PARP;    proline- and arginine-rich protein;   

DOI  :  10.1016/0014-5793(92)80900-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Collagens are typical mosaic proteins containing a number of shuffled domains. These domains have been classified by sequence similarity in order to characterize their structural and functional relationships to other proteins. This analysis provides an overview of homologies of collagen domains. It also reveals two new relationships: (i) a module common to type V, IX, XI, and XII collagens was found to be homologous to the heparin binding domain of thrombospondin; (ii) the modular architecture of a human type VII collagen fragment was identified. Its N-terminal globular domain contains fibronectin type III repeats located adjacent to a Von Willebrand factor type A module. The proposed structural similarities point to analogous subfunctions of the respective domains in otherwise distinct proteins.

【 授权许可】

Unknown