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

@article{Loftus1990AB3,
  title={A beta 3 integrin mutation abolishes ligand binding and alters divalent cation-dependent conformation.},
  author={Joseph C. Loftus and Timothy E. O'Toole and Edward F Plow and Adi Glass and Andrew L Frelinger and M H Ginsberg},
  journal={Science},
  year={1990},
  volume={249 4971},
  pages={915-8}
}
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… CONTINUE READING
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