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| | ==Structure of human regulator of G protein signaling 2 (RGS2) in complex with murine Galpha-q(R183C)== | | ==Structure of human regulator of G protein signaling 2 (RGS2) in complex with murine Galpha-q(R183C)== |
| - | <StructureSection load='4ekc' size='340' side='right' caption='[[4ekc]], [[Resolution|resolution]] 7.40Å' scene=''> | + | <StructureSection load='4ekc' size='340' side='right'caption='[[4ekc]], [[Resolution|resolution]] 7.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4ekc]] is a 4 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=4EKC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EKC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4ekc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EKC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EKC FirstGlance]. <br> |
| - | </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=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ALF:TETRAFLUOROALUMINATE+ION'>ALF</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1agr|1agr]], [[2v4z|2v4z]], [[2af0|2af0]], [[2bcj|2bcj]], [[4ekd|4ekd]]</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=4ekc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ekc OCA], [https://pdbe.org/4ekc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ekc RCSB], [https://www.ebi.ac.uk/pdbsum/4ekc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ekc ProSAT]</span></td></tr> |
| - | <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>
| + | |
| - | <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>
| + | |
| - | <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=4ekc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ekc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ekc RCSB], [http://www.ebi.ac.uk/pdbsum/4ekc PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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> | + | [[https://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> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 4ekc" style="background-color:#fffaf0;"></div> |
| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Guanine nucleotide-binding protein|Guanine nucleotide-binding protein]] | + | *[[Regulator of G-protein signaling 3D structures|Regulator of G-protein signaling 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Heterotrimeric G-protein GTPase]] | |
| | [[Category: Homo sapiens]] | | [[Category: Homo sapiens]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Mus musculus]] | | [[Category: Mus musculus]] |
| - | [[Category: Nance, M R]] | + | [[Category: Nance MR]] |
| - | [[Category: Tesmer, J J.G]] | + | [[Category: Tesmer JJG]] |
| - | [[Category: G protein signaling]]
| + | |
| - | [[Category: Gtp-binding protein fold]]
| + | |
| - | [[Category: Gtpase activation]]
| + | |
| - | [[Category: Homology domain]]
| + | |
| - | [[Category: Regulator]]
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| - | [[Category: Rg]]
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| - | [[Category: Signaling protein-inhibitor complex]]
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| Structural highlights
Function
[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).[1] [2]
Publication Abstract from PubMed
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.
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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Shi G, Partida-Sanchez S, Misra RS, Tighe M, Borchers MT, Lee JJ, Simon MI, Lund FE. Identification of an alternative G{alpha}q-dependent chemokine receptor signal transduction pathway in dendritic cells and granulocytes. J Exp Med. 2007 Oct 29;204(11):2705-18. Epub 2007 Oct 15. PMID:17938235 doi:10.1084/jem.20071267
- ↑ Misra RS, Shi G, Moreno-Garcia ME, Thankappan A, Tighe M, Mousseau B, Kusser K, Becker-Herman S, Hudkins KL, Dunn R, Kehry MR, Migone TS, Marshak-Rothstein A, Simon M, Randall TD, Alpers CE, Liggitt D, Rawlings DJ, Lund FE. G alpha q-containing G proteins regulate B cell selection and survival and are required to prevent B cell-dependent autoimmunity. J Exp Med. 2010 Aug 2;207(8):1775-89. doi: 10.1084/jem.20092735. Epub 2010 Jul, 12. PMID:20624888 doi:10.1084/jem.20092735
- ↑ Nance MR, Kreutz B, Tesmer VM, Sterne-Marr R, Kozasa T, Tesmer JJ. Structural and functional analysis of the regulator of G protein signaling 2-galphaq complex. Structure. 2013 Mar 5;21(3):438-48. doi: 10.1016/j.str.2012.12.016. Epub 2013 Feb, 21. PMID:23434405 doi:10.1016/j.str.2012.12.016
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