1cf1: Difference between revisions

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[[Image:1cf1.gif|left|200px]]
{{Seed}}
[[Image:1cf1.png|left|200px]]


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{{STRUCTURE_1cf1|  PDB=1cf1  |  SCENE=  }}  
{{STRUCTURE_1cf1|  PDB=1cf1  |  SCENE=  }}  


'''ARRESTIN FROM BOVINE ROD OUTER SEGMENTS'''
===ARRESTIN FROM BOVINE ROD OUTER SEGMENTS===




==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.
The line below this paragraph, {{ABSTRACT_PUBMED_10219246}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 10219246 is the PubMed ID number.
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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]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 12:39:48 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:39:41 2008''
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