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1g4m
From Proteopedia
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CRYSTAL STRUCTURE OF BOVINE BETA-ARRESTIN 1
Overview
BACKGROUND: Arrestins are responsible for the desensitization of many, sequence-divergent G protein-coupled receptors. They compete with G, proteins for binding to activated phosphorylated receptors, initiate, receptor internalization, and activate additional signaling pathways., RESULTS: In order to understand the structural basis for receptor binding, and arrestin's function as an adaptor molecule, we determined the X-ray, crystal structure of two truncated forms of bovine beta-arrestin in its, cytosolic inactive state to 1.9 A. Mutational analysis and chimera studies, identify the regions in beta-arrestin responsible for receptor binding, specificity. beta-arrestin demonstrates high structural homology with the, previously solved visual arrestin. All key structural elements responsible, for arrestin's mechanism of activation are conserved. CONCLUSIONS: Based, on structural analysis and mutagenesis data, we propose a previously, unappreciated part in beta-arrestin's mode of action by which a cationic, amphipathic helix may function as a reversible membrane anchor. This novel, activation mechanism would facilitate the formation of a high-affinity, complex between beta-arrestin and an activated receptor regardless of its, specific subtype. Like the interaction between beta-arrestin's polar core, and the phosphorylated receptor, such a general activation mechanism would, contribute to beta-arrestin's versatility as a regulator of many, receptors.
About this Structure
1G4M is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
Crystal structure of beta-arrestin at 1.9 A: possible mechanism of receptor binding and membrane Translocation., Han M, Gurevich VV, Vishnivetskiy SA, Sigler PB, Schubert C, Structure. 2001 Sep;9(9):869-80. PMID:11566136
Page seeded by OCA on Tue Nov 20 15:42:01 2007
