5u1x: Difference between revisions

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 <StructureSection load='5u1x' size='340' side='right'caption='[[5u1x]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5u1x]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ailme Ailme]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5U1X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5U1X FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5u1x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ailuropoda_melanoleuca Ailuropoda melanoleuca]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5U1X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5U1X FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=7RV:N-{[4-(4-PHENYLPIPERAZIN-1-YL)OXAN-4-YL]METHYL}-2-(PHENYLSULFANYL)PYRIDINE-3-CARBOXAMIDE'>7RV</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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]] 3.201&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5u1l|5u1l]], [[5u1u|5u1u]], [[5u1v|5u1v]], [[5u1w|5u1w]], [[5u1y|5u1y]], [[5u2h|5u2h]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=7RV:N-{[4-(4-PHENYLPIPERAZIN-1-YL)OXAN-4-YL]METHYL}-2-(PHENYLSULFANYL)PYRIDINE-3-CARBOXAMIDE'>7RV</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">P2RX7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9646 AILME])</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=5u1x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5u1x OCA], [https://pdbe.org/5u1x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5u1x RCSB], [https://www.ebi.ac.uk/pdbsum/5u1x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5u1x 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=5u1x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5u1x OCA], [http://pdbe.org/5u1x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5u1x RCSB], [http://www.ebi.ac.uk/pdbsum/5u1x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5u1x ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/G1M6C4_AILME G1M6C4_AILME]] Receptor for ATP that acts as a ligand-gated ion channel.[RuleBase:RU000681]
+[https://www.uniprot.org/uniprot/G1M6C4_AILME G1M6C4_AILME] Receptor for ATP that acts as a ligand-gated ion channel.[RuleBase:RU000681]
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The P2X7 receptor is a non-selective cation channel activated by extracellular adenosine triphosphate (ATP). Chronic activation of P2X7 underlies many health problems such as pathologic pain, yet we lack effective antagonists due to poorly understood mechanisms of inhibition. Here we present crystal structures of a mammalian P2X7 receptor complexed with five structurally-unrelated antagonists. Unexpectedly, these drugs all bind to an allosteric site distinct from the ATP-binding pocket in a groove formed between two neighboring subunits. This novel drug-binding pocket accommodates a diversity of small molecules mainly through hydrophobic interactions. Functional assays propose that these compounds allosterically prevent narrowing of the drug-binding pocket and the turret-like architecture during channel opening, which is consistent with a site of action distal to the ATP-binding pocket. These novel mechanistic insights will facilitate the development of P2X7-specific drugs for treating human diseases.
-Structural basis for subtype-specific inhibition of the P2X7 receptor.,Karasawa A, Kawate T Elife. 2016 Dec 9;5. pii: e22153. doi: 10.7554/eLife.22153. PMID:27935479<ref>PMID:27935479</ref>
+==See Also==
+*[[Ion channels 3D structures|Ion channels 3D structures]]
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 5u1x" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Ailme]]
+[[Category: Ailuropoda melanoleuca]]
 [[Category: Large Structures]]
-[[Category: Karasawa, A]]
+[[Category: Karasawa A]]
-[[Category: Kawate, T]]
+[[Category: Kawate T]]
-[[Category: Membrane protein]]
-[[Category: Membrane protein: atp-gated ion channel: allosteric antagonist bound: closed state]]