Ligand recognition by the I domain-containing integrins
- Cite this article as:
- Dickeson, S. & Santoro, S. CMLS, Cell. Mol. Life Sci. (1998) 54: 556. doi:10.1007/s000180050184
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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.