1jsy
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[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== | ||
| Line 7: | Line 16: | ||
==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]] | ||
| Line 18: | Line 27: | ||
[[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
| |||||||
| , resolution 2.9Å | |||||||
|---|---|---|---|---|---|---|---|
| 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
