1cf1: Difference between revisions
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'''ARRESTIN FROM BOVINE ROD OUTER SEGMENTS''' | '''ARRESTIN FROM BOVINE ROD OUTER SEGMENTS''' | ||
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[[Category: Schubert, C.]] | [[Category: Schubert, C.]] | ||
[[Category: Sigler, P B.]] | [[Category: Sigler, P B.]] | ||
[[Category: | [[Category: Binding to acticated and phosphorylated rhodopsin]] | ||
[[Category: | [[Category: Desensitisation of the visual transduction cascade]] | ||
[[Category: | [[Category: Visual arrestin]] | ||
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Revision as of 09:39, 2 May 2008
ARRESTIN FROM BOVINE ROD OUTER SEGMENTS
Overview
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.
About this Structure
1CF1 is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
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 Apr 16;97(2):257-69. PMID:10219246 Page seeded by OCA on Fri May 2 12:39:48 2008
