Analysis of an ascidian integrin provides new insight into early evolution of collagen recognition

FEBS Lett. 2007 May 29;581(13):2434-40. doi: 10.1016/j.febslet.2007.04.054. Epub 2007 Apr 30.

Abstract

AlphaI domain integrins have been found in the ascidian Ciona intestinalis. We produced Ciona alpha1I domain as a recombinant protein. It did not recognize fibril-forming collagens or bind to GFOGER or other similar motifs in triple-helical peptides. No GFOGER motifs were found in Ciona collagens. As Ciona alpha1I bound to collagen IX, we propose that before the emergence of GFOGER-dependent collagen receptors in vertebrates, alphaI domain integrins might have been able to bind to collagen with alternative mechanisms.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Ciona intestinalis / classification*
  • Ciona intestinalis / genetics*
  • Collagen / chemistry
  • Collagen / metabolism*
  • Conserved Sequence
  • Evolution, Molecular*
  • Humans
  • Hydrogen Bonding
  • Integrins / chemistry
  • Integrins / genetics
  • Integrins / physiology*
  • Models, Molecular
  • Molecular Sequence Data
  • Oligopeptides / chemistry
  • Oligopeptides / metabolism
  • Protein Conformation
  • Sequence Alignment

Substances

  • Integrins
  • Oligopeptides
  • Collagen