View source for 4igu


==Crystal structure of the RGS domain of CG5036==
<StructureSection load='4igu' size='340' side='right'caption='[[4igu]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4igu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IGU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IGU FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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=4igu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4igu OCA], [https://pdbe.org/4igu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4igu RCSB], [https://www.ebi.ac.uk/pdbsum/4igu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4igu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8T017_DROME Q8T017_DROME] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Regulator of G protein signaling (RGS) proteins accelerate GTP hydrolysis on G protein alpha subunits, restricting their activity downstream from G protein-coupled receptors. Here we identify Drosophila Double hit (Dhit) as a dual RGS regulator of Galphao. In addition to the conventional GTPase-activating action, Dhit possesses the guanine nucleotide dissociation inhibitor (GDI) activity, slowing the rate of GTP uptake by Galphao; both activities are mediated by the same RGS domain. These findings are recapitulated using homologous mammalian Galphao/i proteins and RGS19. Crystal structure and mutagenesis studies provide clues into the molecular mechanism for this unprecedented GDI activity. Physiologically, we confirm this activity in Drosophila asymmetric cell divisions and HEK293T cells. We show that the oncogenic Galphao mutant found in breast cancer escapes this GDI regulation. Our studies identify Dhit and its homologs as double-action regulators, inhibiting Galphao/i proteins both through suppression of their activation and acceleration of their inactivation through the single RGS domain.

Double suppression of the Galpha protein activity by RGS proteins.,Lin C, Koval A, Tishchenko S, Gabdulkhakov A, Tin U, Solis GP, Katanaev VL Mol Cell. 2014 Feb 20;53(4):663-71. doi: 10.1016/j.molcel.2014.01.014. PMID:24560274<ref>PMID:24560274</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4igu" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Drosophila melanogaster]]
[[Category: Large Structures]]
[[Category: Gabdulkhakov A]]
[[Category: Tishchenko S]]