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| | <StructureSection load='2oj4' size='340' side='right'caption='[[2oj4]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='2oj4' size='340' side='right'caption='[[2oj4]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2oj4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OJ4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OJ4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2oj4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OJ4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OJ4 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RGS3 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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]] 2.3Å</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=2oj4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oj4 OCA], [https://pdbe.org/2oj4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2oj4 RCSB], [https://www.ebi.ac.uk/pdbsum/2oj4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2oj4 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=2oj4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oj4 OCA], [https://pdbe.org/2oj4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2oj4 RCSB], [https://www.ebi.ac.uk/pdbsum/2oj4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2oj4 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/RGS3_HUMAN RGS3_HUMAN]] Down-regulates signaling from heterotrimeric G-proteins by increasing the GTPase activity of the alpha subunits, thereby driving them into their inactive GDP-bound form. Down-regulates G-protein-mediated release of inositol phosphates and activation of MAP kinases.<ref>PMID:8602223</ref> <ref>PMID:9858594</ref> <ref>PMID:10749886</ref> <ref>PMID:11294858</ref>
| + | [https://www.uniprot.org/uniprot/RGS3_HUMAN RGS3_HUMAN] Down-regulates signaling from heterotrimeric G-proteins by increasing the GTPase activity of the alpha subunits, thereby driving them into their inactive GDP-bound form. Down-regulates G-protein-mediated release of inositol phosphates and activation of MAP kinases.<ref>PMID:8602223</ref> <ref>PMID:9858594</ref> <ref>PMID:10749886</ref> <ref>PMID:11294858</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oj/2oj4_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oj/2oj4_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Boura, E]] | + | [[Category: Boura E]] |
| - | [[Category: Obsil, T]] | + | [[Category: Obsil T]] |
| - | [[Category: Protein]]
| + | |
| - | [[Category: Rgs domain]]
| + | |
| - | [[Category: Signaling protein inhibitor]]
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| Structural highlights
Function
RGS3_HUMAN Down-regulates signaling from heterotrimeric G-proteins by increasing the GTPase activity of the alpha subunits, thereby driving them into their inactive GDP-bound form. Down-regulates G-protein-mediated release of inositol phosphates and activation of MAP kinases.[1] [2] [3] [4]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Regulator of G protein signaling (RGS) proteins function as GTPase-activating proteins (GAPs) for the alpha-subunit of heterotrimeric G proteins. Several RGS proteins have been found to interact with 14-3-3 proteins. The 14-3-3 protein binding inhibits the GAP function of RGS proteins presumably by blocking their interaction with G(alpha) subunit. Since RGS proteins interact with G(alpha) subunits through their RGS domains, it is reasonable to assume that the 14-3-3 protein can either sterically occlude the G(alpha) interaction surface of RGS domain and/or change its structure. In this work, we investigated whether the 14-3-3 protein binding affects the structure of RGS3 using the time-resolved tryptophan fluorescence spectroscopy. Two single-tryptophan mutants of RGS3 were used to study conformational changes of RGS3 molecule. Our measurements revealed that the 14-3-3 protein binding induces structural changes in both the N-terminal part and the C-terminal RGS domain of phosphorylated RGS3 molecule. Experiments with the isolated RGS domain of RGS3 suggest that this domain alone can, to some extent, interact with the 14-3-3 protein in a phosphorylation-independent manner. In addition, a crystal structure of the RGS domain of RGS3 was solved at 2.3A resolution. The data obtained from the resolution of the structure of the RGS domain suggest that the 14-3-3 protein-induced conformational change affects the region within the G(alpha)-interacting portion of the RGS domain. This can explain the inhibitory effect of the 14-3-3 protein on GAP activity of RGS3.
14-3-3 protein interacts with and affects the structure of RGS domain of regulator of G protein signaling 3 (RGS3).,Rezabkova L, Boura E, Herman P, Vecer J, Bourova L, Sulc M, Svoboda P, Obsilova V, Obsil T J Struct Biol. 2010 Jun;170(3):451-61. Epub 2010 Mar 27. PMID:20347994[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Druey KM, Blumer KJ, Kang VH, Kehrl JH. Inhibition of G-protein-mediated MAP kinase activation by a new mammalian gene family. Nature. 1996 Feb 22;379(6567):742-6. PMID:8602223 doi:http://dx.doi.org/10.1038/379742a0
- ↑ Dulin NO, Sorokin A, Reed E, Elliott S, Kehrl JH, Dunn MJ. RGS3 inhibits G protein-mediated signaling via translocation to the membrane and binding to Galpha11. Mol Cell Biol. 1999 Jan;19(1):714-23. PMID:9858594
- ↑ Dulin NO, Pratt P, Tiruppathi C, Niu J, Voyno-Yasenetskaya T, Dunn MJ. Regulator of G protein signaling RGS3T is localized to the nucleus and induces apoptosis. J Biol Chem. 2000 Jul 14;275(28):21317-23. PMID:10749886 doi:http://dx.doi.org/10.1074/jbc.M910079199
- ↑ Shi CS, Lee SB, Sinnarajah S, Dessauer CW, Rhee SG, Kehrl JH. Regulator of G-protein signaling 3 (RGS3) inhibits Gbeta1gamma 2-induced inositol phosphate production, mitogen-activated protein kinase activation, and Akt activation. J Biol Chem. 2001 Jun 29;276(26):24293-300. Epub 2001 Apr 9. PMID:11294858 doi:http://dx.doi.org/10.1074/jbc.M100089200
- ↑ Rezabkova L, Boura E, Herman P, Vecer J, Bourova L, Sulc M, Svoboda P, Obsilova V, Obsil T. 14-3-3 protein interacts with and affects the structure of RGS domain of regulator of G protein signaling 3 (RGS3). J Struct Biol. 2010 Jun;170(3):451-61. Epub 2010 Mar 27. PMID:20347994 doi:10.1016/j.jsb.2010.03.009
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