1scg: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
 
(7 intermediate revisions by the same user not shown)
Line 1: Line 1:
{{Theoretical_model}}
{{Theoretical_model}}


[[Image:1scg.png|left|200px]]
==PAIR OF THEORETICAL MODELS FOR THE S. CEREVISIAE G PROTEIN HETEROTRIMER, BASED ON THE COORDINATES OF THE MAMMALIAN G PROTEIN==
<StructureSection load='1scg' size='340' side='right'caption='[[1scg]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SCG FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1scg FirstGlance], [https://www.ebi.ac.uk/pdbsum/1scg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1scg ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystallographic structure of the G protein heterotrimer Gi alpha 1(GDP)beta 1 gamma 2 (at 2.3 A) reveals two nonoverlapping regions of contact between alpha and beta, an extended interface between beta and nearly all of gamma, and limited interaction of alpha with gamma. The major alpha/beta interface covers switch II of alpha, and GTP-induced rearrangement of switch II causes subunit dissociation during signaling. Alterations in GDP binding in the heterotrimer (compared with alpha-GDP) explain stabilization of the inactive conformation of alpha by beta gamma. Repeated WD motifs in beta form a circularized sevenfold beta propeller. The conserved cores of these motifs are a scaffold for display of their more variable linkers on the exterior face of each propeller blade.


{{STRUCTURE_1scg|  PDB=1scg  |  SCENE=  }}
The structure of the G protein heterotrimer Gi alpha 1 beta 1 gamma 2.,Wall MA, Coleman DE, Lee E, Iniguez-Lluhi JA, Posner BA, Gilman AG, Sprang SR Cell. 1995 Dec 15;83(6):1047-58. PMID:8521505<ref>PMID:8521505</ref>


===PAIR OF THEORETICAL MODELS FOR THE S. CEREVISIAE G PROTEIN HETEROTRIMER, BASED ON THE COORDINATES OF THE MAMMALIAN G PROTEIN===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_8521505}}
<div class="pdbe-citations 1scg" style="background-color:#fffaf0;"></div>
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:008521505</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Theoretical Model]]
[[Category: Large Structures]]
[[Category: Gaitatzes, C G]]
[[Category: Gaitatzes, C G]]
[[Category: Neer, E J]]
[[Category: Neer, E J]]
[[Category: Smith, T F]]
[[Category: Smith, T F]]

Latest revision as of 07:29, 22 September 2021

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

PAIR OF THEORETICAL MODELS FOR THE S. CEREVISIAE G PROTEIN HETEROTRIMER, BASED ON THE COORDINATES OF THE MAMMALIAN G PROTEIN

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA