Distinct ligand binding sites in the I domain of integrin alpha M beta 2 that differentially affect a divalent cation-dependent conformation.

@article{McGuire1995DistinctLB,
  title={Distinct ligand binding sites in the I domain of integrin alpha M beta 2 that differentially affect a divalent cation-dependent conformation.},
  author={Sarah Lea McGuire and Mary Lynn Bajt},
  journal={The Journal of biological chemistry},
  year={1995},
  volume={270 43},
  pages={
          25866-71
        }
}
The I domains of the leukocyte beta 2 integrins have been shown to be essential for ligand recognition. Amino acid substitutions of Asp140 and Ser142, which reside in a conserved cluster of oxygenated residues, abrogate divalent cation ligand binding function of alpha M beta 2. Presently, we evaluated the role of two I domain regions in alpha M beta 2 ligand recognition: 1) the conserved cluster of oxygenated residues (Asp134, Asp140, Ser142, and Ser144) and 2) a 7-amino acid region (Phe246… CONTINUE READING
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