1scg
From Proteopedia
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- | + | {{Theoretical_model}} | |
- | + | ==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. | ||
- | + | 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> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
+ | <div class="pdbe-citations 1scg" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Theoretical Model]] | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Gaitatzes, C G]] | ||
+ | [[Category: Neer, E J]] | ||
+ | [[Category: Smith, T F]] |
Current revision
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
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