3q85

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<StructureSection load='3q85' size='340' side='right'caption='[[3q85]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
<StructureSection load='3q85' size='340' side='right'caption='[[3q85]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3q85]] is a 2 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=3Q85 FirstGlance]. <br>
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<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>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.757&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2dpx|2dpx]], [[3cbq|3cbq]], [[3q72|3q72]], [[3q7p|3q7p]], [[3q7q|3q7q]]</div></td></tr>
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<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>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Rem2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
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<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'>[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>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/REM2_MOUSE REM2_MOUSE]] Binds GTP saturably and exhibits a low intrinsic rate of GTP hydrolysis.
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[https://www.uniprot.org/uniprot/REM2_MOUSE REM2_MOUSE] Binds GTP saturably and exhibits a low intrinsic rate of GTP hydrolysis.
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<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&reg;/PubMed&reg;, 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 3D structures|GTP-binding protein 3D structures]]
*[[GTP-binding protein 3D structures|GTP-binding protein 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Lk3 transgenic mice]]
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[[Category: Mus musculus]]
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[[Category: Hirsch, J A]]
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[[Category: Hirsch JA]]
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[[Category: Navon-Perry, L]]
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[[Category: Navon-Perry L]]
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[[Category: Cav2 beta]]
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[[Category: G-domain]]
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[[Category: G-protein]]
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[[Category: Signaling protein]]
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Current revision

Crystal Structure of Rem2 G-domain -GTP Analog Complex

PDB ID 3q85

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