1ayr: Difference between revisions

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{{STRUCTURE_1ayr|  PDB=1ayr  |  SCENE=  }}  
{{STRUCTURE_1ayr|  PDB=1ayr  |  SCENE=  }}  


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




==Overview==
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Retinal arrestin is the essential protein for the termination of the light response in vertebrate rod outer segments. It plays an important role in quenching the light-induced enzyme cascade by its ability to bind to phosphorylated light-activated rhodopsin (P-Rh*). Arrestins are found in various G-protein-coupled amplification cascades. Here we report on the three-dimensional structure of bovine arrestin (relative molecular mass, 45,300) at 3.3 A resolution. The crystal structure comprises two domains of antiparallel beta-sheets connected through a hinge region and one short alpha-helix on the back of the amino-terminal fold. The binding region for phosphorylated light-activated rhodopsin is located at the N-terminal domain, as indicated by the docking of the photoreceptor to the three-dimensional structure of arrestin. This agrees with the interpretation of binding studies on partially digested and mutated arrestin.
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==About this Structure==
==About this Structure==
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[[Category: Rhodopsin]]
[[Category: Rhodopsin]]
[[Category: Sensory transduction]]
[[Category: Sensory transduction]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 10:51:26 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:52:49 2008''

Revision as of 14:52, 30 June 2008

File:1ayr.png

Template:STRUCTURE 1ayr

ARRESTIN FROM BOVINE ROD OUTER SEGMENTS

Template:ABSTRACT PUBMED 9495348

About this Structure

1AYR is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

X-ray crystal structure of arrestin from bovine rod outer segments., Granzin J, Wilden U, Choe HW, Labahn J, Krafft B, Buldt G, Nature. 1998 Feb 26;391(6670):918-21. PMID:9495348

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