Corpus ID: 33411974

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={A. Mould and J. A. Askari and S. Barton and A. Kline and P. McEwan and S. E. Craig and M. Humphries},
  journal={The Journal of biological chemistry},
  year={2002},
  volume={277 22},
  pages={
          19800-5
        }
}
  • A. Mould, J. A. Askari, +4 authors M. Humphries
  • Published 2002
  • Medicine
  • The Journal of biological chemistry
  • 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

    Topics from this paper.

    Relating conformation to function in integrin α5β1
    • 65
    • PDF
    How the headpiece hinge angle is opened: new insights into the dynamics of integrin activation
    • 171
    • Highly Influenced
    • PDF