1jsy
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jsy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jsy OCA], [http://www.ebi.ac.uk/pdbsum/1jsy PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jsy RCSB]</span> | ||
}} | }} | ||
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[[Category: nonvisual arrestin]] | [[Category: nonvisual arrestin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:38:33 2008'' |
Revision as of 18:38, 30 March 2008
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| , resolution 2.9Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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