1cf1
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="1cf1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cf1, resolution 2.8Å" /> '''ARRESTIN FROM BOVINE ...)
Next diff →
Revision as of 10:17, 20 November 2007
|
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 Tue Nov 20 12:24:21 2007
