1gdd: Difference between revisions

Revision as of 05:07, 1 July 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:1gdd.png

Template:STRUCTURE 1gdd

TERTIARY AND QUATERNARY STRUCTURAL CHANGES IN GIA1 INDUCED BY GTP HYDROLYSISTERTIARY AND QUATERNARY STRUCTURAL CHANGES IN GIA1 INDUCED BY GTP HYDROLYSIS

Template:ABSTRACT PUBMED 7481799

About this StructureAbout this Structure

1GDD is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

ReferenceReference

Tertiary and quaternary structural changes in Gi alpha 1 induced by GTP hydrolysis., Mixon MB, Lee E, Coleman DE, Berghuis AM, Gilman AG, Sprang SR, Science. 1995 Nov 10;270(5238):954-60. PMID:7481799

Page seeded by OCA on Tue Jul 1 05:07:53 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1gdd.jpg|left|200px]]
+{{Seed}}
+[[Image:1gdd.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1gdd|  PDB=1gdd  |  SCENE=  }}
-'''TERTIARY AND QUATERNARY STRUCTURAL CHANGES IN GIA1 INDUCED BY GTP HYDROLYSIS'''
+===TERTIARY AND QUATERNARY STRUCTURAL CHANGES IN GIA1 INDUCED BY GTP HYDROLYSIS===
-==Overview==
+<!--
-Crystallographic analysis of 2.2 angstrom resolution shows that guanosine triphosphate (GTP) hydrolysis triggers conformational changes in the heterotrimeric G-protein alpha subunit, Gi alpha 1. The switch II and switch III segments become disordered, and linker II connecting the Ras and alpha helical domains moves, thus altering the structures of potential effector and beta gamma binding regions. Contacts between the alpha-helical and Ras domains are weakened, possibly facilitating the release of guanosine diphosphate (GDP). The amino and carboxyl termini, which contain receptor and beta gamma binding determinants, are disordered in the complex with GTP, but are organized into a compact microdomain on GDP hydrolysis. The amino terminus also forms extensive quaternary contacts with neighboring alpha subunits in the lattice, suggesting that multimers of alpha subunits or heterotrimers may play a role in signal transduction.
+The line below this paragraph, {{ABSTRACT_PUBMED_7481799}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 7481799 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_7481799}}
 ==About this Structure==
@@ Line 25: / Line 29: @@
 [[Category: Sprang, S R.]]
 [[Category: Gtp-ase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 17:26:24 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 05:07:53 2008''