5u2h: Difference between revisions
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<StructureSection load='5u2h' size='340' side='right'caption='[[5u2h]], [[Resolution|resolution]] 3.90Å' scene=''> | <StructureSection load='5u2h' size='340' side='right'caption='[[5u2h]], [[Resolution|resolution]] 3.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5u2h]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5u2h]] is a 2 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=5U2H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5U2H FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=7S1:N-CYANO-N-[(1R)-1-PHENYLETHYL]-N-QUINOLIN-5-YLGUANIDINE'>7S1</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.903Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=7S1:N-CYANO-N-[(1R)-1-PHENYLETHYL]-N-QUINOLIN-5-YLGUANIDINE'>7S1</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=5u2h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5u2h OCA], [https://pdbe.org/5u2h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5u2h RCSB], [https://www.ebi.ac.uk/pdbsum/5u2h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5u2h ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 20: | Line 19: | ||
</div> | </div> | ||
<div class="pdbe-citations 5u2h" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5u2h" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Ion channels 3D structures|Ion channels 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Ailuropoda melanoleuca]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Karasawa | [[Category: Karasawa A]] | ||
[[Category: Kawate | [[Category: Kawate T]] | ||
Latest revision as of 07:45, 21 November 2024
Crystal structure of the ATP-gated P2X7 ion channel bound to ATP and allosteric antagonist A804598Crystal structure of the ATP-gated P2X7 ion channel bound to ATP and allosteric antagonist A804598
Structural highlights
FunctionG1M6C4_AILME Receptor for ATP that acts as a ligand-gated ion channel.[RuleBase:RU000681] Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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