Ligand recognition by the I domain-containing integrins
Rent the article at a discountRent now
* Final gross prices may vary according to local VAT.Get Access
Seven of the integrin α subunits described to date, α 1 , α 2 , α L , α X , α d , α M and α E , 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 α M and α L 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.
- Ligand recognition by the I domain-containing integrins
Cellular and Molecular Life Sciences CMLS
Volume 54, Issue 6 , pp 556-566
- Cover Date
- Print ISSN
- Online ISSN
- Birkhäuser Verlag
- Additional Links
- Key words. Adhesion; integrin; I domain; divalent cation; ligand recognition.
- Industry Sectors