Identification of a contact domain between echistatin and the integrin alpha(v)beta(3) by photoaffinity cross-linking.

@article{Scheibler2001IdentificationOA,
  title={Identification of a contact domain between echistatin and the integrin alpha(v)beta(3) by photoaffinity cross-linking.},
  author={Lukas Christoph Scheibler and Dale F. Mierke and Gal Bitan and Michael S Rosenblatt and Michael Chorev},
  journal={Biochemistry},
  year={2001},
  volume={40 50},
  pages={
          15117-26
        }
}
The integrin alpha(v)beta(3) is the major receptor mediating the attachment of osteoclasts to the extracellular matrix in bone and plays a critical role in bone resorption and bone remodeling. Most of the ligands interacting with the alpha(v)beta(3) receptor contain an Arg-Gly-Asp (RGD) motif. Recently, we have identified two small RGD peptides, containing a benzophenone moiety at either the carboxyl or amino terminus, that photo-cross-linked within the beta(3)[99-118] [Bitan, G., et al. (1999… CONTINUE READING