5svt

<StructureSection load='5svt' size='340' side='right' caption='[[5svt]], [[Resolution|resolution]] 3.79&Aring;' scene=''>

<table><tr><td colspan='2'>[[5svt]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5SVT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5SVT FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5svj|5svj]], [[5svk|5svk]], [[5svl|5svl]], [[5svm|5svm]], [[5svp|5svp]], [[5svq|5svq]], [[5svr|5svr]], [[5svs|5svs]]</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=5svt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5svt OCA], [http://pdbe.org/5svt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5svt RCSB], [http://www.ebi.ac.uk/pdbsum/5svt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5svt ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/P2RX3_HUMAN P2RX3_HUMAN]] Receptor for ATP that acts as a ligand-gated ion channel.

P2X receptors are trimeric, non-selective cation channels activated by ATP that have important roles in the cardiovascular, neuronal and immune systems. Despite their central function in human physiology and although they are potential targets of therapeutic agents, there are no structures of human P2X receptors. The mechanisms of receptor desensitization and ion permeation, principles of antagonism, and complete structures of the pore-forming transmembrane domains of these receptors remain unclear. Here we report X-ray crystal structures of the human P2X3 receptor in apo/resting, agonist-bound/open-pore, agonist-bound/closed-pore/desensitized and antagonist-bound/closed states. The open state structure harbours an intracellular motif we term the 'cytoplasmic cap', which stabilizes the open state of the ion channel pore and creates lateral, phospholipid-lined cytoplasmic fenestrations for water and ion egress. The competitive antagonists TNP-ATP and A-317491 stabilize the apo/resting state and reveal the interactions responsible for competitive inhibition. These structures illuminate the conformational rearrangements that underlie P2X receptor gating and provide a foundation for the development of new pharmacological agents.

 

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== References ==

[[Category: Gouaux, E]]

[[Category: Lu, W]]

[[Category: Mansoor, S E]]

[[Category: Oosterheert, W]]

[[Category: Shekhar, M]]

[[Category: Tajkhorshid, E]]

[[Category: Anomalous signal]]

[[Category: Ion channel]]

[[Category: Membrane protein]]