Abstract
The ligand-binding function of integrin adhesion receptors depends on divalent cations. A mutant αIIbβ3 integrin (platelet gpIIb/IIIa) that lacks ligand recognition shows immunologic evidence ofa 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 β3 subunit. This residue is proximal to bound ligand and is in a conserved region among integrins that are enriched in oxygenated residues. The spacing ofthese 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.
Original language | English (US) |
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Pages (from-to) | 915-918 |
Number of pages | 4 |
Journal | Science |
Volume | 249 |
Issue number | 4971 |
DOIs | |
State | Published - 1990 |
ASJC Scopus subject areas
- General