5f1c: Difference between revisions
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The | ==Crystal structure of an invertebrate P2X receptor from the Gulf Coast tick in the presence of ATP and Zn2+ ion at 2.9 Angstroms== | ||
<StructureSection load='5f1c' size='340' side='right' caption='[[5f1c]], [[Resolution|resolution]] 2.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5f1c]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F1C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5F1C FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=5f1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f1c OCA], [http://pdbe.org/5f1c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f1c RCSB], [http://www.ebi.ac.uk/pdbsum/5f1c PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
P2X receptors are trimeric ATP-gated cation channels involved in physiological processes ranging widely from neurotransmission to pain and taste signal transduction. The modulation of the channel gating, including that by divalent cations, contributes to these diverse physiological functions of P2X receptors. Here, we report the crystal structure of an invertebrate P2X receptor from the Gulf Coast tick Amblyomma maculatum in the presence of ATP and Zn(2+) ion, together with electrophysiological and computational analyses. The structure revealed two distinct metal binding sites, M1 and M2, in the extracellular region. The M1 site, located at the trimer interface, is responsible for Zn(2+) potentiation by facilitating the structural change of the extracellular domain for pore opening. In contrast, the M2 site, coupled with the ATP binding site, might contribute to regulation by Mg(2+). Overall, our work provides structural insights into the divalent cation modulations of P2X receptors. | |||
Structural Insights into Divalent Cation Modulations of ATP-Gated P2X Receptor Channels.,Kasuya G, Fujiwara Y, Takemoto M, Dohmae N, Nakada-Nakura Y, Ishitani R, Hattori M, Nureki O Cell Rep. 2016 Feb 2;14(4):932-44. doi: 10.1016/j.celrep.2015.12.087. Epub 2016, Jan 21. PMID:26804916<ref>PMID:26804916</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
[[Category: | <div class="pdbe-citations 5f1c" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Hattori, M]] | |||
[[Category: Ishitani, R]] | [[Category: Ishitani, R]] | ||
[[Category: Kasuya, G]] | [[Category: Kasuya, G]] | ||
[[Category: Nureki, O]] | |||
[[Category: Agonist]] | |||
[[Category: Channel]] | |||
[[Category: Complex]] | |||
[[Category: Ligand]] | |||
[[Category: Membrane protein]] | |||
Revision as of 06:49, 11 May 2016
Crystal structure of an invertebrate P2X receptor from the Gulf Coast tick in the presence of ATP and Zn2+ ion at 2.9 AngstromsCrystal structure of an invertebrate P2X receptor from the Gulf Coast tick in the presence of ATP and Zn2+ ion at 2.9 Angstroms
Structural highlights
Publication Abstract from PubMedP2X receptors are trimeric ATP-gated cation channels involved in physiological processes ranging widely from neurotransmission to pain and taste signal transduction. The modulation of the channel gating, including that by divalent cations, contributes to these diverse physiological functions of P2X receptors. Here, we report the crystal structure of an invertebrate P2X receptor from the Gulf Coast tick Amblyomma maculatum in the presence of ATP and Zn(2+) ion, together with electrophysiological and computational analyses. The structure revealed two distinct metal binding sites, M1 and M2, in the extracellular region. The M1 site, located at the trimer interface, is responsible for Zn(2+) potentiation by facilitating the structural change of the extracellular domain for pore opening. In contrast, the M2 site, coupled with the ATP binding site, might contribute to regulation by Mg(2+). Overall, our work provides structural insights into the divalent cation modulations of P2X receptors. Structural Insights into Divalent Cation Modulations of ATP-Gated P2X Receptor Channels.,Kasuya G, Fujiwara Y, Takemoto M, Dohmae N, Nakada-Nakura Y, Ishitani R, Hattori M, Nureki O Cell Rep. 2016 Feb 2;14(4):932-44. doi: 10.1016/j.celrep.2015.12.087. Epub 2016, Jan 21. PMID:26804916[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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