1g4m: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
Line 1: Line 1:
[[Image:1g4m.jpg|left|200px]]
{{Seed}}
[[Image:1g4m.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1g4m|  PDB=1g4m  |  SCENE=  }}  
{{STRUCTURE_1g4m|  PDB=1g4m  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF BOVINE BETA-ARRESTIN 1'''
===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.
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.
-->
{{ABSTRACT_PUBMED_11566136}}


==About this Structure==
==About this Structure==
Line 26: Line 30:
[[Category: Alternative splicing]]
[[Category: Alternative splicing]]
[[Category: Sensory transduction]]
[[Category: Sensory transduction]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:07:57 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 04:24:18 2008''

Revision as of 01:24, 1 July 2008

File:1g4m.png

Template:STRUCTURE 1g4m

CRYSTAL STRUCTURE OF BOVINE BETA-ARRESTIN 1

Template:ABSTRACT PUBMED 11566136

About this Structure

1G4M 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 04:24:18 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1g4m&oldid=600477"