This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1g4m

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
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

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

Personal tools