4igu: Difference between revisions
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== Structural highlights == | == 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> | <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> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</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> | <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> | </table> | ||
Latest revision as of 17:16, 8 November 2023
Crystal structure of the RGS domain of CG5036Crystal structure of the RGS domain of CG5036
Structural highlights
FunctionPublication Abstract from PubMedRegulator 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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