1g4r
From Proteopedia
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| - | [[Image:1g4r.gif|left|200px]] | + | [[Image:1g4r.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF BOVINE BETA-ARRESTIN 1''' | + | {{Structure |
| + | |PDB= 1g4r |SIZE=350|CAPTION= <scene name='initialview01'>1g4r</scene>, resolution 2.20Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''CRYSTAL STRUCTURE OF BOVINE BETA-ARRESTIN 1''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1G4R is a [ | + | 1G4R 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=1G4R OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11566136 11566136] |
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Han, M.]] | [[Category: Han, M.]] | ||
[[Category: Schubert, C.]] | [[Category: Schubert, C.]] | ||
| - | [[Category: g-protein coupled | + | [[Category: g-protein coupled receptor]] |
| - | [[Category: g- | + | [[Category: g-protein]] |
[[Category: signal transduction]] | [[Category: signal transduction]] | ||
| - | ''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 11:18:11 2008'' |
Revision as of 09:18, 20 March 2008
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| , resolution 2.20Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
1G4R 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
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