The 2.8 A crystal structure of visual arrestin: a model for arrestin's regulation.

Hirsch JA, Schubert C, Gurevich VV, Sigler PB
Cell. 1999 97 (2): 257-69

PMID: 10219246 · DOI:10.1016/s0092-8674(00)80735-7

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.

MeSH Terms (13)

Amino Acid Sequence Animals Arrestin Cattle Crystallography, X-Ray Dimerization Humans Models, Molecular Molecular Sequence Data Protein Conformation Recombinant Proteins Sequence Homology, Amino Acid Static Electricity

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