1ayr | pdb_00001ayr
ARRESTIN FROM BOVINE ROD OUTER SEGMENTS
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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
Page seeded by OCA on Tue Nov 20 11:12:45 2007
