Integrin activation involves a conformational change in the alpha 1 helix of the beta subunit A-domain.

@article{Mould2002IntegrinAI,
  title={Integrin activation involves a conformational change in the alpha 1 helix of the beta subunit A-domain.},
  author={Andrew Mould and Janet A. Askari and Stephanie J. Barton and Adam D Kline and Paul A. McEwan and Susan E. Craig and Martin J Humphries},
  journal={The Journal of biological chemistry},
  year={2002},
  volume={277 22},
  pages={19800-5}
}
The ligand-binding region of integrin beta subunits contains a von Willebrand factor type A-domain: an alpha/beta "Rossmann" fold containing a metal ion-dependent adhesion site (MIDAS) on its top face. Although there is evidence to suggest that the betaA-domain undergoes changes in tertiary structure during receptor activation, the identity of the secondary structure elements that change position is unknown. The mAb 12G10 recognizes a unique cation-regulated epitope on the beta(1) A-domain… CONTINUE READING

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