Open AccessThe collαgen III fibril has a “flexi-rod” structure of flexible sequences interspersed with rigid bioactive domains including two with hemostatic roles
Author(s) -
John Parkin,
James D. San Antonio,
Anton V. Persikov,
Hayat Dagher,
Raymond Dalgleish,
Shane T. Jensen,
Xavier Jeunemaı̂tre,
Judy Savige
Publication year - 2017
Publication title -
plos one
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.99
H-Index - 332
ISSN - 1932-6203
DOI - 10.1371/journal.pone.0175582
Subject(s) - fibrillogenesis , fibril , chemistry , integrin , biophysics , von willebrand factor , glycoprotein , platelet membrane glycoprotein , plasma protein binding , binding site , microbiology and biotechnology , biochemistry , platelet , biology , cell , immunology
Collagen III is critical to the integrity of blood vessels and distensible organs, and in hemostasis. Examination of the human collagen III interactome reveals a nearly identical structural arrangement and charge distribution pattern as for collagen I, with cell interaction domains, fibrillogenesis and enzyme cleavage domains, several major ligand-binding regions, and intermolecular crosslink sites at the same sites. These similarities allow heterotypic fibril formation with, and substitution by, collagen I in embryonic development and wound healing. The collagen III fibril assumes a “flexi-rod” structure with flexible zones interspersed with rod-like domains, which is consistent with the molecule’s prominence in young, pliable tissues and distensible organs. Collagen III has two major hemostasis domains, with binding motifs for von Willebrand factor, α2β1 integrin, platelet binding octapeptide and glycoprotein VI, consistent with the bleeding tendency observed with COL3A1 disease-causing sequence variants.