1ayr
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(New page: 200px<br /><applet load="1ayr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ayr, resolution 3.3Å" /> '''ARRESTIN FROM BOVINE ...)
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Revision as of 09:05, 20 November 2007
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ARRESTIN FROM BOVINE ROD OUTER SEGMENTS
Overview
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.
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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