Crystal structure of beta-arrestin at 1.9 A: possible mechanism of receptor binding and membrane Translocation.
Han, M., Gurevich, V.V., Vishnivetskiy, S.A., Sigler, P.B., Schubert, C.(2001) Structure 9: 869-880
- PubMed: 11566136 
- DOI: https://doi.org/10.1016/s0969-2126(01)00644-x
- Primary Citation of Related Structures:  
1G4M, 1G4R - PubMed Abstract: 
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.
Organizational Affiliation: 
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA. mhan@mpi.com