1cf1
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY= | ||
+ | |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]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''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
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, resolution 2.8Å | |||||||
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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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