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Structural constraints on the evolution of the collagen fibril: convergence on a 1014-residue COL domain.


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Authors

Slatter, David Anthony 
Farndale, Richard William 

Abstract

Type I collagen is the fundamental component of the extracellular matrix. Its α1 gene is the direct descendant of ancestral fibrillar collagen and contains 57 exons encoding the rod-like triple-helical COL domain. We trace the evolution of the COL domain from a primordial collagen 18 residues in length to its present 1014 residues, the limit of its possible length. In order to maintain and improve the essential structural features of collagen during evolution, exons can be added or extended only in permitted, non-random increments that preserve the position of spatially sensitive cross-linkage sites. Such sites cannot be maintained unless the twist of the triple helix is close to 30 amino acids per turn. Inspection of the gene structure of other long structural proteins, fibronectin and titin, suggests that their evolution might have been subject to similar constraints.

Description

Keywords

D-period, collagen, cross-links, exon structure, Amino Acid Sequence, Amino Acids, Animals, Biological Evolution, Collagen, Humans, Models, Molecular, Protein Conformation, Protein Interaction Domains and Motifs

Journal Title

Open Biol

Conference Name

Journal ISSN

2046-2441
2046-2441

Volume Title

5

Publisher

The Royal Society
Sponsorship
British Heart Foundation (None)
British Heart Foundation (None)
British Heart Foundation (RG/15/4/31268)
The work was funded by a project grant to D.A.S. and R.W.F. from British Heart Foundation (PG/08/011/24416). R.W.F. was supported by BHF Programme grant nos. (RG/09/003/27122 and RG/15/4/31268).