1jsy
From Proteopedia
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[[Image:1jsy.gif|left|200px]] | [[Image:1jsy.gif|left|200px]] | ||
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'''Crystal structure of bovine arrestin-2''' | '''Crystal structure of bovine arrestin-2''' | ||
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[[Category: Milano, S K.]] | [[Category: Milano, S K.]] | ||
[[Category: Pace, H C.]] | [[Category: Pace, H C.]] | ||
| - | [[Category: | + | [[Category: Beta-arrestin]] |
| - | [[Category: | + | [[Category: Desensitization]] |
| - | [[Category: | + | [[Category: Down-regulation]] |
| - | [[Category: | + | [[Category: Endocytosis]] |
| - | [[Category: | + | [[Category: Nonvisual arrestin]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:52:10 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 18:52, 2 May 2008
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 Page seeded by OCA on Fri May 2 21:52:10 2008
