1ayr
From Proteopedia
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| , resolution 3.3Å | |||||||
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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
Page seeded by OCA on Thu Mar 20 10:04:03 2008
