1jsy: Difference between revisions
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[[Image:1jsy.gif|left|200px]] | [[Image:1jsy.gif|left|200px]] | ||
'''Crystal structure of bovine arrestin-2''' | {{Structure | ||
|PDB= 1jsy |SIZE=350|CAPTION= <scene name='initialview01'>1jsy</scene>, resolution 2.9Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Crystal structure of bovine arrestin-2''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1JSY is a [ | 1JSY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JSY OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11876640 11876640] | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Milano, S K.]] | [[Category: Milano, S K.]] | ||
[[Category: Pace, H C.]] | [[Category: Pace, H C.]] | ||
[[Category: beta- | [[Category: beta-arrestin]] | ||
[[Category: desensitization]] | [[Category: desensitization]] | ||
[[Category: down-regulation]] | [[Category: down-regulation]] | ||
[[Category: endocytosis]] | [[Category: endocytosis]] | ||
[[Category: nonvisual | [[Category: nonvisual arrestin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:08:00 2008'' | ||
Revision as of 10:08, 20 March 2008
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| 1jsy, resolution 2.9Å | |||||||||||||
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| 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
Page seeded by OCA on Thu Mar 20 12:08:00 2008
