1cf1

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cf1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cf1 OCA], [http://www.ebi.ac.uk/pdbsum/1cf1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cf1 RCSB]</span>
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[[Category: visual arrestin]]
[[Category: visual arrestin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:20:24 2008''

Revision as of 16:20, 30 March 2008


PDB ID 1cf1

Drag the structure with the mouse to rotate
, resolution 2.8Å
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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

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