1azt: Difference between revisions

Revision as of 17:56, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1azt.png

Template:STRUCTURE 1azt

GS-ALPHA COMPLEXED WITH GTP-GAMMA-SGS-ALPHA COMPLEXED WITH GTP-GAMMA-S

Template:ABSTRACT PUBMED 9395396

About this StructureAbout this Structure

1AZT is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the adenylyl cyclase activator Gsalpha., Sunahara RK, Tesmer JJ, Gilman AG, Sprang SR, Science. 1997 Dec 12;278(5345):1943-7. PMID:9395396

Page seeded by OCA on Mon Jun 30 17:56:00 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1azt.jpg|left|200px]]
+{{Seed}}
+[[Image:1azt.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1azt|  PDB=1azt  |  SCENE=  }}
-'''GS-ALPHA COMPLEXED WITH GTP-GAMMA-S'''
+===GS-ALPHA COMPLEXED WITH GTP-GAMMA-S===
-==Overview==
+<!--
-The crystal structure of Gsalpha, the heterotrimeric G protein alpha subunit that stimulates adenylyl cyclase, was determined at 2.5 A in a complex with guanosine 5'-O-(3-thiotriphosphate) (GTPgammaS). Gsalpha is the prototypic member of a family of GTP-binding proteins that regulate the activities of effectors in a hormone-dependent manner. Comparison of the structure of Gsalpha.GTPgammaS with that of Gialpha.GTPgammaS suggests that their effector specificity is primarily dictated by the shape of the binding surface formed by the switch II helix and the alpha3-beta5 loop, despite the high sequence homology of these elements. In contrast, sequence divergence explains the inability of regulators of G protein signaling to stimulate the GTPase activity of Gsalpha. The betagamma binding surface of Gsalpha is largely conserved in sequence and structure to that of Gialpha, whereas differences in the surface formed by the carboxyl-terminal helix and the alpha4-beta6 loop may mediate receptor specificity.
+The line below this paragraph, {{ABSTRACT_PUBMED_9395396}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9395396 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9395396}}
 ==About this Structure==
@@ Line 27: / Line 31: @@
 [[Category: Hydrolase]]
 [[Category: Signal transducing protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 10:53:27 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:56:00 2008''