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| - | [[Image:1g4r.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1g4r| PDB=1g4r | SCENE= }} | | {{STRUCTURE_1g4r| PDB=1g4r | SCENE= }} |
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| - | '''CRYSTAL STRUCTURE OF BOVINE BETA-ARRESTIN 1'''
| + | ===CRYSTAL STRUCTURE OF BOVINE BETA-ARRESTIN 1=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11566136}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11566136 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11566136}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: G-protein]] | | [[Category: G-protein]] |
| | [[Category: Signal transduction]] | | [[Category: Signal transduction]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:08:16 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 04:24:37 2008'' |
Revision as of 01:24, 1 July 2008
Template:STRUCTURE 1g4r
CRYSTAL STRUCTURE OF BOVINE BETA-ARRESTIN 1
Template:ABSTRACT PUBMED 11566136
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
Page seeded by OCA on Tue Jul 1 04:24:37 2008
