Cellular and Molecular Life Sciences CMLS

, Volume 54, Issue 6, pp 556–566

Ligand recognition by the I domain-containing integrins

  • S. K. Dickeson
  • S. A. Santoro

DOI: 10.1007/s000180050184

Cite this article as:
Dickeson, S. & Santoro, S. CMLS, Cell. Mol. Life Sci. (1998) 54: 556. doi:10.1007/s000180050184

Abstract.

Seven of the integrin α subunits described to date, α1 , α2 , αL , αX , αd , αM and αE , contain a highly conserved I (or A) domain of approximately 200 amino acid residues inserted near the amino-terminus of the subunit. As the result of a variety of independent experimental approaches, a large body of data has recently accumulated that indicates that the I domains are independent, autonomously folding domains capable of directly binding ligands that play a necessary and important role in ligand binding by the intact integrins. Recent crystallographic studies have elucidated the structures of recombinant αM and αL I domains and also delineated a novel divalent cation-binding motif within the I domains (metal ion-dependent adhesion site, MIDAS) that appears to mediate the divalent cation binding of the I domains and the I domain-containing integrins to their ligands.

Key words. Adhesion; integrin; I domain; divalent cation; ligand recognition. 

Copyright information

© Birkhäuser Verlag Basel, 1998

Authors and Affiliations

  • S. K. Dickeson
    • 1
  • S. A. Santoro
    • 1
  1. 1.Department of Pathology, Box 8118, Washington University School of Medicine, 660 South Euclid Avenue, St. Louis (Missouri 63110, USA), Fax +1 314 362 3016, e-mail: santoro@labmed.wustl.eduUS