4ekd

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{{STRUCTURE_4ekd| PDB=4ekd | SCENE= }}
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==Structure of human regulator of G protein signaling 2 (RGS2) in complex with murine Galpha-q(R183C)==
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===Structure of human regulator of G protein signaling 2 (RGS2) in complex with murine Galpha-q(R183C)===
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<StructureSection load='4ekd' size='340' side='right' caption='[[4ekd]], [[Resolution|resolution]] 2.71&Aring;' scene=''>
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{{ABSTRACT_PUBMED_23434405}}
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4ekd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EKD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EKD FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ALF:TETRAFLUOROALUMINATE+ION'>ALF</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1agr|1agr]], [[2v4z|2v4z]], [[2af0|2af0]], [[2bcj|2bcj]], [[4ekc|4ekc]]</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Gnaq ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]), RGS2, G0S8, GIG31 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Heterotrimeric_G-protein_GTPase Heterotrimeric G-protein GTPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.5.1 3.6.5.1] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ekd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ekd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ekd RCSB], [http://www.ebi.ac.uk/pdbsum/4ekd PDBsum]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The heterotrimeric G protein Galphaq is a key regulator of blood pressure, and excess Galphaq signaling leads to hypertension. A specific inhibitor of Galphaq is the GTPase activating protein (GAP) known as regulator of G protein signaling 2 (RGS2). The molecular basis for how Galphaq/11 subunits serve as substrates for RGS proteins and how RGS2 mandates its selectivity for Galphaq is poorly understood. In crystal structures of the RGS2-Galphaq complex, RGS2 docks to Galphaq in a different orientation from that observed in RGS-Galphai/o complexes. Despite its unique pose, RGS2 maintains canonical interactions with the switch regions of Galphaq in part because its alpha6 helix adopts a distinct conformation. We show that RGS2 forms extensive interactions with the alpha-helical domain of Galphaq that contribute to binding affinity and GAP potency. RGS subfamilies that do not serve as GAPs for Galphaq are unlikely to form analogous stabilizing interactions.
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==Function==
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Structural and functional analysis of the regulator of G protein signaling 2-galphaq complex.,Nance MR, Kreutz B, Tesmer VM, Sterne-Marr R, Kozasa T, Tesmer JJ Structure. 2013 Mar 5;21(3):438-48. doi: 10.1016/j.str.2012.12.016. Epub 2013 Feb, 21. PMID:23434405<ref>PMID:23434405</ref>
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[[http://www.uniprot.org/uniprot/GNAQ_MOUSE GNAQ_MOUSE]] Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Regulates B-cell selection and survival and is required to prevent B-cell-dependent autoimmunity. Regulates chemotaxis of BM-derived neutrophils and dendritic cells (in vitro).<ref>PMID:17938235</ref> <ref>PMID:20624888</ref> [[http://www.uniprot.org/uniprot/RGS2_HUMAN RGS2_HUMAN]] Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. May play a role in leukemogenesis. Plays a role in negative feedback control pathway for adenylyl cyclase signaling. Binds EIF2B5 and blocks its activity, thereby inhibiting the translation of mRNA into protein.<ref>PMID:11278586</ref> <ref>PMID:17901199</ref> <ref>PMID:7643615</ref> <ref>PMID:19736320</ref>
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[4ekd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EKD OCA].
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</div>
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==Reference==
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==See Also==
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<ref group="xtra">PMID:023434405</ref><references group="xtra"/><references/>
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*[[Guanine nucleotide-binding protein|Guanine nucleotide-binding protein]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Heterotrimeric G-protein GTPase]]
[[Category: Heterotrimeric G-protein GTPase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Nance, M R.]]
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[[Category: Nance, M R]]
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[[Category: Tesmer, J J.G.]]
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[[Category: Tesmer, J J.G]]
[[Category: Gtp-binding]]
[[Category: Gtp-binding]]
[[Category: Gtpase activation]]
[[Category: Gtpase activation]]

Revision as of 11:08, 21 December 2014

Structure of human regulator of G protein signaling 2 (RGS2) in complex with murine Galpha-q(R183C)

4ekd, resolution 2.71Å

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