The 2.8 A crystal structure of visual arrestin: a model for arrestin's regulation.
Hirsch, J.A., Schubert, C., Gurevich, V.V., Sigler, P.B.(1999) Cell 97: 257-269
- PubMed: 10219246 
- DOI: https://doi.org/10.1016/s0092-8674(00)80735-7
- Primary Citation of Related Structures:  
1CF1 - PubMed Abstract: 
G protein-coupled signaling is utilized by a wide variety of eukaryotes for communicating information from the extracellular environment. Signal termination is achieved by the action of the arrestins, which bind to activated, phosphorylated G protein-coupled receptors. We describe here crystallographic studies of visual arrestin in its basal conformation. The salient features of the structure are a bipartite molecule with an unusual polar core. This core is stabilized in part by an extended carboxy-terminal tail that locks the molecule into an inactive state. In addition, arrestin is found to be a dimer of two asymmetric molecules, suggesting an intrinsic conformational plasticity. In conjunction with biochemical and mutagenesis data, we propose a molecular mechanism by which arrestin is activated for receptor binding.
Organizational Affiliation: 
Howard Hughes Medical Institute, Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06511, USA.