6ah5: Difference between revisions
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==Structure of human P2X3 receptor in complex with ATP and Mg2+ ion== | |||
<StructureSection load='6ah5' size='340' side='right'caption='[[6ah5]], [[Resolution|resolution]] 3.82Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6ah5]] is a 3 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=6AH5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6AH5 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.819Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PRD_900001:alpha-maltose'>PRD_900001</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=6ah5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ah5 OCA], [https://pdbe.org/6ah5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ah5 RCSB], [https://www.ebi.ac.uk/pdbsum/6ah5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ah5 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/P2RX3_HUMAN P2RX3_HUMAN] Receptor for ATP that acts as a ligand-gated ion channel. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
P2X3 receptor channels expressed in sensory neurons are activated by extracellular ATP and serve important roles in nociception and sensory hypersensitization, making them attractive therapeutic targets. Although several P2X3 structures are known, it is unclear how physiologically abundant Ca(2+)-ATP and Mg(2+)-ATP activate the receptor, or how divalent cations regulate channel function. We used structural, computational and functional approaches to show that a crucial acidic chamber near the nucleotide-binding pocket in human P2X3 receptors accommodates divalent ions in two distinct modes in the absence and presence of nucleotide. The unusual engagement between the receptor, divalent ion and the gamma-phosphate of ATP enables channel activation by ATP-divalent complex, cooperatively stabilizes the nucleotide on the receptor to slow ATP unbinding and recovery from desensitization, a key mechanism for limiting channel activity. These findings reveal how P2X3 receptors recognize and are activated by divalent-bound ATP, aiding future physiological investigations and drug development. | |||
Molecular mechanisms of human P2X3 receptor channel activation and modulation by divalent cation bound ATP.,Li M, Wang Y, Banerjee R, Marinelli F, Silberberg S, Faraldo-Gomez JD, Hattori M, Swartz KJ Elife. 2019 Jun 24;8. pii: 47060. doi: 10.7554/eLife.47060. PMID:31232692<ref>PMID:31232692</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Hattori | <div class="pdbe-citations 6ah5" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Ion channels 3D structures|Ion channels 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Hattori M]] | |||