Regulation of integrin function: evidence that bivalent-cation-induced conformational changes lead to the unmasking of ligand-binding sites within integrin alpha5 beta1.

@article{Mould1998RegulationOI,
  title={Regulation of integrin function: evidence that bivalent-cation-induced conformational changes lead to the unmasking of ligand-binding sites within integrin alpha5 beta1.},
  author={A. Paul Mould and Alistair N. Garratt and Wilma Puzon-McLaughlin and Yoshikazu Takada and Martin J. Humphries},
  journal={The Biochemical journal},
  year={1998},
  volume={331 ( Pt 3)},
  pages={
          821-8
        }
}
The molecular mechanisms that regulate integrin-ligand binding are unknown; however, bivalent cations are essential for integrin activity. According to recent models of integrin tertiary structure, sites involved in ligand recognition are located on the upper face of the seven-bladed beta-propeller formed by the N-terminal repeats of the alpha subunit and on the von Willebrand factor A-domain-like region of the beta subunit. The epitopes of function-altering monoclonal antibodies (mAbs) cluster… CONTINUE READING

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