A beta 3 integrin mutation abolishes ligand binding and alters divalent cation-dependent conformation - PubMed (original) (raw)

Comparative Study

. 1990 Aug 24;249(4971):915-8.

doi: 10.1126/science.2392682.

Affiliations

• PMID: 2392682
• DOI: 10.1126/science.2392682

Comparative Study

A beta 3 integrin mutation abolishes ligand binding and alters divalent cation-dependent conformation

J C Loftus et al. Science. 1990.

Abstract

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 and is in a conserved region among integrins that are enriched in oxygenated residues. The spacing of these residues aligns with the calcium-binding residues in EF hand proteins, suggesting interaction with receptor-bound divalent cation as a mechanism of ligand binding common to all integrins.

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