Crystal structure of beta-arrestin at 1.9 A: possible mechanism of receptor binding and membrane Translocation.

@article{Han2001CrystalSO,
  title={Crystal structure of beta-arrestin at 1.9 A: possible mechanism of receptor binding and membrane Translocation.},
  author={M Han and Vsevolod V. Gurevich and Sergey A. Vishnivetskiy and Paul B. Sigler and Carsten Schubert},
  journal={Structure},
  year={2001},
  volume={9 9},
  pages={869-80}
}
BACKGROUND Arrestins are responsible for the desensitization of many sequence-divergent G protein-coupled receptors. They compete with G proteins for binding to activated phosphorylated receptors, initiate receptor internalization, and activate additional signaling pathways. RESULTS In order to understand the structural basis for receptor binding and arrestin's function as an adaptor molecule, we determined the X-ray crystal structure of two truncated forms of bovine beta-arrestin in its… CONTINUE READING