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| ==Crystal Structure of Rem2 G-domain -GTP Analog Complex== | | ==Crystal Structure of Rem2 G-domain -GTP Analog Complex== |
- | <StructureSection load='3q85' size='340' side='right' caption='[[3q85]], [[Resolution|resolution]] 1.76Å' scene=''> | + | <StructureSection load='3q85' size='340' side='right'caption='[[3q85]], [[Resolution|resolution]] 1.76Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[3q85]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q85 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3Q85 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3q85]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q85 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3Q85 FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</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]] 1.757Å</td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2dpx|2dpx]], [[3cbq|3cbq]], [[3q72|3q72]], [[3q7p|3q7p]], [[3q7q|3q7q]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</scene></td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Rem2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=3q85 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q85 OCA], [https://pdbe.org/3q85 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3q85 RCSB], [https://www.ebi.ac.uk/pdbsum/3q85 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3q85 ProSAT]</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=3q85 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q85 OCA], [http://pdbe.org/3q85 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3q85 RCSB], [http://www.ebi.ac.uk/pdbsum/3q85 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3q85 ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[http://www.uniprot.org/uniprot/REM2_MOUSE REM2_MOUSE]] Binds GTP saturably and exhibits a low intrinsic rate of GTP hydrolysis. | + | [https://www.uniprot.org/uniprot/REM2_MOUSE REM2_MOUSE] Binds GTP saturably and exhibits a low intrinsic rate of GTP hydrolysis. |
- | <div style="background-color:#fffaf0;">
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- | == Publication Abstract from PubMed ==
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- | The RGK family of small G-proteins, including Rad, Gem, Rem1, and Rem2, is inducibly expressed in various mammalian tissues and interacts with voltage-dependent calcium channels and Rho kinase. Many questions remain regarding their physiological roles and molecular mechanism. Previous crystallographic studies reported RGK G-domain:guanosine di-phosphate structures. To test whether RGK proteins undergo a nucleotide-induced conformational change, we determined the crystallographic structures of Rad:GppNHp and Rem2:GppNHp to 1.7 and 1.8 A resolutions, respectively. Also, we characterized the nucleotide-binding properties and conformations for Gem, Rad, and several structure-based mutants using fluorescence spectroscopy. The results suggest that RGK G-proteins may not behave as Ras-like canonical nucleotide-induced molecular switches. Further, the RGK proteins have differing structures and nucleotide-binding properties, which may have implications for their varied action on effectors.
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- | RGK Family G-Domain:GTP Analog Complex Structures and Nucleotide-Binding Properties.,Sasson Y, Navon-Perry L, Huppert D, Hirsch JA J Mol Biol. 2011 Aug 29. PMID:21903096<ref>PMID:21903096</ref>
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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- | </div>
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- | <div class="pdbe-citations 3q85" style="background-color:#fffaf0;"></div>
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| ==See Also== | | ==See Also== |
- | *[[GTP-binding protein|GTP-binding protein]] | + | *[[GTP-binding protein 3D structures|GTP-binding protein 3D structures]] |
- | == References ==
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- | <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Lk3 transgenic mice]] | + | [[Category: Large Structures]] |
- | [[Category: Hirsch, J A]] | + | [[Category: Mus musculus]] |
- | [[Category: Navon-Perry, L]] | + | [[Category: Hirsch JA]] |
- | [[Category: Cav2 beta]] | + | [[Category: Navon-Perry L]] |
- | [[Category: G-domain]]
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- | [[Category: G-protein]]
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- | [[Category: Signaling protein]]
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