The crucial role of trimerization domains in collagen folding.

Boudko SP, Engel J, Bächinger HP
Int J Biochem Cell Biol. 2012 44 (1): 21-32

PMID: 22001560 · DOI:10.1016/j.biocel.2011.09.009

Collagens contain large numbers of Gly-Xaa-Yaa peptide repeats that form the characteristic triple helix, where the individual chains fold into a polyproline II helix and three of these helices form a right-handed triple helix. For the proper folding of the triple helix collagens contain trimerization domains. These domains ensure a single starting point for triple helix formation and are also responsible for the chain selection in heterotrimeric collagens. Trimerization domains are non-collagenous domains of very different structures. The size of trimerization domains varies from 35 residues in type IX collagen to around 250 residues for the fibrillar collagens. These domains are not only crucial for biological functions, but they are also attractive tools for generating recombinant collagen fragments of interest as well as for general use in protein engineering and biomaterial design. Here we review the current knowledge of the structure and function of these trimerization domains.

Copyright © 2011 Elsevier Ltd. All rights reserved.

MeSH Terms (12)

Amino Acid Sequence Circular Dichroism Collagen Collagen Type IV Collagen Type VIII Collagen Type X Humans Models, Molecular Molecular Sequence Data Protein Conformation Protein Folding Protein Structure, Tertiary

Connections (1)

This publication is referenced by other Labnodes entities:

Links