1jsy

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1jsy, resolution 2.9Å

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Crystal structure of bovine arrestin-2

Overview

Arrestin binding to activated, phosphorylated G protein-coupled receptors, (GPCRs) represents a critical step in regulation of light- and, hormone-dependent signaling. Nonvisual arrestins, such as arrestin-2, interact with multiple proteins for the purpose of propagating and, terminating signaling events. Using a combination of X-ray, crystallography, molecular modeling, mutagenesis, and binding analysis, we, reveal structural features of arrestin-2 that may enable simultaneous, binding to phosphorylated receptor, SH3 domains, phosphoinositides, and, beta-adaptin. The structure of full-length arrestin-2 thus provides a, uniquely oriented scaffold for assembly of multiple, diverse molecules, involved in GPCR signal transduction.

About this Structure

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

Reference

Scaffolding functions of arrestin-2 revealed by crystal structure and mutagenesis., Milano SK, Pace HC, Kim YM, Brenner C, Benovic JL, Biochemistry. 2002 Mar 12;41(10):3321-8. PMID:11876640

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