1cf1

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{{STRUCTURE_1cf1| PDB=1cf1 | SCENE= }}
{{STRUCTURE_1cf1| PDB=1cf1 | SCENE= }}
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'''ARRESTIN FROM BOVINE ROD OUTER SEGMENTS'''
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===ARRESTIN FROM BOVINE ROD OUTER SEGMENTS===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_10219246}}
==About this Structure==
==About this Structure==
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[[Category: Desensitisation of the visual transduction cascade]]
[[Category: Desensitisation of the visual transduction cascade]]
[[Category: Visual arrestin]]
[[Category: Visual arrestin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:39:48 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:39:41 2008''

Revision as of 17:39, 30 June 2008

Image:1cf1.png

Template:STRUCTURE 1cf1

ARRESTIN FROM BOVINE ROD OUTER SEGMENTS

Template:ABSTRACT PUBMED 10219246

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

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