3q7q: Difference between revisions

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 ==Crystal Structure of Rad G-domain Q148A-GTP Analog Complex==
-<StructureSection load='3q7q' size='340' side='right' caption='[[3q7q]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+<StructureSection load='3q7q' size='340' side='right'caption='[[3q7q]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3q7q]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q7Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3Q7Q FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3q7q]] is a 2 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=3Q7Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3Q7Q FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.3&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2dpx|2dpx]], [[3q72|3q72]], [[3q7p|3q7p]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RRAD, RAD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3q7q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q7q OCA], [https://pdbe.org/3q7q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3q7q RCSB], [https://www.ebi.ac.uk/pdbsum/3q7q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3q7q 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=3q7q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q7q OCA], [http://pdbe.org/3q7q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3q7q RCSB], [http://www.ebi.ac.uk/pdbsum/3q7q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3q7q ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/RAD_HUMAN RAD_HUMAN]] May play an important role in cardiac antiarrhythmia via the strong suppression of voltage-gated L-type Ca(2+) currents. Regulates voltage-dependent L-type calcium channel subunit alpha-1C trafficking to the cell membrane (By similarity). Inhibits cardiac hypertrophy through the calmodulin-dependent kinase II (CaMKII) pathway. Inhibits phosphorylation and activation of CAMK2D.<ref>PMID:18056528</ref>
+[https://www.uniprot.org/uniprot/RAD_HUMAN RAD_HUMAN] May play an important role in cardiac antiarrhythmia via the strong suppression of voltage-gated L-type Ca(2+) currents. Regulates voltage-dependent L-type calcium channel subunit alpha-1C trafficking to the cell membrane (By similarity). Inhibits cardiac hypertrophy through the calmodulin-dependent kinase II (CaMKII) pathway. Inhibits phosphorylation and activation of CAMK2D.<ref>PMID:18056528</ref>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-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.
-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>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3q7q" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[GTP-binding protein|GTP-binding protein]]
+*[[GTP-binding protein 3D structures|GTP-binding protein 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
-[[Category: Hirsch, J A]]
+[[Category: Large Structures]]
-[[Category: Navon-Perry, L]]
+[[Category: Hirsch JA]]
-[[Category: Sasson, Y]]
+[[Category: Navon-Perry L]]
-[[Category: Cav2 beta]]
+[[Category: Sasson Y]]
-[[Category: G-domain]]
-[[Category: G-protein]]
-[[Category: Signaling protein]]