Ligand binding to integrin alphaIIbbeta3 is dependent on a MIDAS-like domain in the beta3 subunit.

@article{Tozer1996LigandBT,
  title={Ligand binding to integrin alphaIIbbeta3 is dependent on a MIDAS-like domain in the beta3 subunit.},
  author={E C Tozer and Robert C. Liddington and Michael J. Sutcliffe and A H Smeeton and Joseph C. Loftus},
  journal={The Journal of biological chemistry},
  year={1996},
  volume={271 36},
  pages={21978-84}
}
Substitution of beta3 residue Asp119, Ser121, or Ser123 results in a loss of the ligand binding function of integrin alphaIIbbeta3. Homologous residues in other integrin beta subunits are similarly critical for ligand binding function. This DXSXS motif is also present in the I domain of certain integrin alpha subunits, where it constitutes a portion of the unique metal ion-dependent adhesion site (MIDAS). In this report, we have utilized the crystal structure of the recombinant alphaM I domain… CONTINUE READING

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