2ht6: Difference between revisions

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 ==Crystal structure of Human Gem G-domain bound to GDP==
-<StructureSection load='2ht6' size='340' side='right' caption='[[2ht6]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
+<StructureSection load='2ht6' size='340' side='right'caption='[[2ht6]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2ht6]] 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=2HT6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2HT6 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2ht6]] 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=2HT6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HT6 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</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]] 2.4&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GEM, KIR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=2ht6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ht6 OCA], [http://pdbe.org/2ht6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ht6 RCSB], [http://www.ebi.ac.uk/pdbsum/2ht6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ht6 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=2ht6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ht6 OCA], [https://pdbe.org/2ht6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ht6 RCSB], [https://www.ebi.ac.uk/pdbsum/2ht6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ht6 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/GEM_HUMAN GEM_HUMAN]] Could be a regulatory protein, possibly participating in receptor-mediated signal transduction at the plasma membrane. Has guanine nucleotide-binding activity but undetectable intrinsic GTPase activity.
+[https://www.uniprot.org/uniprot/GEM_HUMAN GEM_HUMAN] Could be a regulatory protein, possibly participating in receptor-mediated signal transduction at the plasma membrane. Has guanine nucleotide-binding activity but undetectable intrinsic GTPase activity.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 20: / Line 20: @@
 </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2ht6 ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Gem, a member of the Rad,Gem/Kir subfamily of small G-proteins, has unique sequence features. We report here the crystallographic structure determination of the Gem G-domain in complex with nucleotide to 2.4 A resolution. Although the basic Ras protein fold is maintained, the Gem switch regions emphatically differ from the Ras paradigm. Our ensuing biochemical characterization indicates that Gem G-domain markedly prefers GDP over GTP. Two known functions of Gem are distinctly affected by spatially separated clusters of mutations.
-Structure-function studies of the G-domain from human gem, a novel small G-protein.,Opatowsky Y, Sasson Y, Shaked I, Ward Y, Chomsky-Hecht O, Litvak Y, Selinger Z, Kelly K, Hirsch JA FEBS Lett. 2006 Oct 30;580(25):5959-64. Epub 2006 Oct 6. PMID:17052716<ref>PMID:17052716</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 2ht6" 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: Opatowsky, Y]]
+[[Category: Hirsch JA]]
-[[Category: Signaling protein]]
+[[Category: Opatowsky Y]]
-[[Category: Small g-protein]]