A β 3 Integrin Mutation Abolishes Ligand Binding and Alters Divalent Cation-Dependent Conformation

• DOI: 10.1126/science.2392682
• Publication Date: 2006-10-05T22:10:14Z
• Authors: Joseph C. Loftus; Timothy E. O'Toole; Edward F. Plow; Alison Glass; Andrew L. Frelinger; Mark H. Ginsberg
• Keywords: Divalent

The ligand-binding function of integrin adhesion receptors depends on divalent cations. A mutant α IIb β 3 (platelet gpIIb/IIIa) that lacks ligand recognition shows immunologic evidence a perturbed interaction with This was found to be caused by G → T mutation resulted in an Asp 119 Tyr substitution the subunit. residue is proximal bound and conserved region among integrins are enriched oxygenated residues. spacing these residues aligns calcium-binding EF hand proteins, suggesting receptor-bound cation as mechanism binding common all integrins.