1g4m: Difference between revisions
New page: left|200px<br /><applet load="1g4m" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g4m, resolution 1.90Å" /> '''CRYSTAL STRUCTURE OF... |
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[[Image:1g4m.jpg|left|200px]]<br /><applet load="1g4m" size=" | [[Image:1g4m.jpg|left|200px]]<br /><applet load="1g4m" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1g4m, resolution 1.90Å" /> | caption="1g4m, resolution 1.90Å" /> | ||
'''CRYSTAL STRUCTURE OF BOVINE BETA-ARRESTIN 1'''<br /> | '''CRYSTAL STRUCTURE OF BOVINE BETA-ARRESTIN 1'''<br /> | ||
==Overview== | ==Overview== | ||
BACKGROUND: Arrestins are responsible for the desensitization of many | 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== | ==About this Structure== | ||
1G4M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http:// | 1G4M is a [http://en.wikipedia.org/wiki/Single_protein 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=1G4M OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: sensory transduction]] | [[Category: sensory transduction]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:46:02 2008'' | ||
Revision as of 10:46, 21 February 2008
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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
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
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