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]] 2.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3q7q]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/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> | |||
<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='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 Homo sapiens])</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://www.rcsb.org/pdb/explore.do?structureId=3q7q RCSB], [http://www.ebi.ac.uk/pdbsum/3q7q PDBsum]</span></td></tr> | |||
</table> | |||
<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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[GTP-binding protein|GTP-binding protein]] | *[[GTP-binding protein|GTP-binding protein]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Hirsch, J A | [[Category: Hirsch, J A]] | ||
[[Category: Navon-Perry, L | [[Category: Navon-Perry, L]] | ||
[[Category: Sasson, Y | [[Category: Sasson, Y]] | ||
[[Category: Cav2 beta]] | [[Category: Cav2 beta]] | ||
[[Category: G-domain]] | [[Category: G-domain]] | ||
[[Category: G-protein]] | [[Category: G-protein]] | ||
[[Category: Signaling protein]] | [[Category: Signaling protein]] | ||
Revision as of 16:05, 9 December 2014
Crystal Structure of Rad G-domain Q148A-GTP Analog ComplexCrystal Structure of Rad G-domain Q148A-GTP Analog Complex
Structural highlights
Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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