5an8

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'''Unreleased structure'''
 
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The entry 5an8 is ON HOLD until Paper Publication
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==Cryo-electron microscopy structure of rabbit TRPV2 ion channel==
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<SX load='5an8' size='340' side='right' viewer='molstar' caption='[[5an8]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5an8]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AN8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AN8 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.8&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5an8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5an8 OCA], [https://pdbe.org/5an8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5an8 RCSB], [https://www.ebi.ac.uk/pdbsum/5an8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5an8 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/G1SNM3_RABIT G1SNM3_RABIT]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Transient receptor potential vanilloid (TRPV) cation channels are polymodal sensors involved in a variety of physiological processes. TRPV2, a member of the TRPV family, is regulated by temperature, by ligands, such as probenecid and cannabinoids, and by lipids. TRPV2 has been implicated in many biological functions, including somatosensation, osmosensation and innate immunity. Here we present the atomic model of rabbit TRPV2 in its putative desensitized state, as determined by cryo-EM at a nominal resolution of approximately 4 A. In the TRPV2 structure, the transmembrane segment 6 (S6), which is involved in gate opening, adopts a conformation different from the one observed in TRPV1. Structural comparisons of TRPV1 and TRPV2 indicate that a rotation of the ankyrin-repeat domain is coupled to pore opening via the TRP domain, and this pore opening can be modulated by rearrangements in the secondary structure of S6.
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Authors: Zubcevic, L., Herzik, M.A.J., Chung, B.C., Lander, G.C., Lee, S.Y.
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Cryo-electron microscopy structure of the TRPV2 ion channel.,Zubcevic L, Herzik MA Jr, Chung BC, Liu Z, Lander GC, Lee SY Nat Struct Mol Biol. 2016 Jan 18. doi: 10.1038/nsmb.3159. PMID:26779611<ref>PMID:26779611</ref>
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Description: Electron cryo-microscopy of a TRPV2 channel
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Zubcevic, L]]
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<div class="pdbe-citations 5an8" style="background-color:#fffaf0;"></div>
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[[Category: Lander, G.C]]
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[[Category: Chung, B.C]]
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==See Also==
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[[Category: Lee, S.Y]]
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*[[Ion channels 3D structures|Ion channels 3D structures]]
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[[Category: Herzik, M.A.J]]
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== References ==
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<references/>
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__TOC__
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</SX>
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[[Category: Large Structures]]
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[[Category: Oryctolagus cuniculus]]
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[[Category: Chung BC]]
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[[Category: Herzik MAJ]]
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[[Category: Lander GC]]
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[[Category: Lee SY]]
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[[Category: Zubcevic L]]

Current revision

Cryo-electron microscopy structure of rabbit TRPV2 ion channel

5an8, resolution 3.80Å

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