Article
A beta 3 integrin mutation abolishes ligand binding and alters divalent cation-dependent conformation.
Science (New York, N.Y.) - 24 Aug 1990
Loftus J C, O'Toole T E, Plow E F, Glass A, Frelinger A L, Ginsberg M H
Abstract excerpt
The ligand-binding function of integrin adhesion receptors depends on divalent cations. A mutant alpha IIb beta 3 integrin (platelet gpIIb/IIIa) that lacks ligand recognition shows immunologic evidence of a perturbed interaction with divalent cations. This was found to be caused by a G----T mutation that resulted in an Asp119----Tyr119 substitution in the beta 3 subunit. This residue is proximal to bound ligand...
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