3j5q
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 3j5q is ON HOLD Authors: Cao E, Liao M, Cheng Y, Julius D Description: Structure of TRPV1 ion channel in complex with DkTx and RTX determined by si...) |
|||
| (11 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Structure of TRPV1 ion channel in complex with DkTx and RTX determined by single particle electron cryo-microscopy== | |
| + | <SX load='3j5q' size='340' side='right' viewer='molstar' caption='[[3j5q]], [[Resolution|resolution]] 3.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3j5q]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Chilobrachys_guangxiensis Chilobrachys guangxiensis] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J5Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3J5Q FirstGlance]. <br> | ||
| + | </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=3j5q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j5q OCA], [https://pdbe.org/3j5q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3j5q RCSB], [https://www.ebi.ac.uk/pdbsum/3j5q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3j5q ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/TRPV1_RAT TRPV1_RAT] Receptor-activated non-selective calcium permeant cation channel involved in detection of noxious chemical and thermal stimuli. Seems to mediate proton influx and may be involved in intracellular acidosis in nociceptive neurons. May be involved in mediation of inflammatory pain and hyperalgesia. Sensitized by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases, which involves PKC isozymes and PCL. Activation by vanilloids, like capsaicin, and temperatures higher than 42 degrees Celsius, exhibits a time- and Ca(2+)-dependent outward rectification, followed by a long-lasting refractory state. Mild extracellular acidic pH (6.5) potentiates channel activation by noxious heat and vanilloids, whereas acidic conditions (pH <6) directly activate the channel. Can be activated by endogenous compounds, including 12-hydroperoxytetraenoic acid and bradykinin. Acts as ionotropic endocannabinoid receptor with central neuromodulatory effects. Triggers a form of long-term depression (TRPV1-LTD) mediated by the endocannabinoid anandamine in the hippocampus and nucleus accumbens by affecting AMPA receptors endocytosis.<ref>PMID:9349813</ref> <ref>PMID:10644739</ref> <ref>PMID:11140687</ref> <ref>PMID:11418861</ref> <ref>PMID:12095983</ref> <ref>PMID:12194871</ref> <ref>PMID:12808128</ref> <ref>PMID:14523239</ref> <ref>PMID:12764195</ref> <ref>PMID:14630912</ref> <ref>PMID:15173182</ref> <ref>PMID:21076423</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Transient receptor potential (TRP) channels are polymodal signal detectors that respond to a wide range of physical and chemical stimuli. Elucidating how these channels integrate and convert physiological signals into channel opening is essential to understanding how they regulate cell excitability under normal and pathophysiological conditions. Here we exploit pharmacological probes (a peptide toxin and small vanilloid agonists) to determine structures of two activated states of the capsaicin receptor, TRPV1. A domain (consisting of transmembrane segments 1-4) that moves during activation of voltage-gated channels remains stationary in TRPV1, highlighting differences in gating mechanisms for these structurally related channel superfamilies. TRPV1 opening is associated with major structural rearrangements in the outer pore, including the pore helix and selectivity filter, as well as pronounced dilation of a hydrophobic constriction at the lower gate, suggesting a dual gating mechanism. Allosteric coupling between upper and lower gates may account for rich physiological modulation exhibited by TRPV1 and other TRP channels. | ||
| - | + | TRPV1 structures in distinct conformations reveal activation mechanisms.,Cao E, Liao M, Cheng Y, Julius D Nature. 2013 Dec 5;504(7478):113-8. doi: 10.1038/nature12823. PMID:24305161<ref>PMID:24305161</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 3j5q" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Ion channels 3D structures|Ion channels 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </SX> | ||
| + | [[Category: Chilobrachys guangxiensis]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Rattus norvegicus]] | ||
| + | [[Category: Cao E]] | ||
| + | [[Category: Cheng Y]] | ||
| + | [[Category: Julius D]] | ||
| + | [[Category: Liao M]] | ||
Current revision
Structure of TRPV1 ion channel in complex with DkTx and RTX determined by single particle electron cryo-microscopy
| |||||||||
