6aei
From Proteopedia
(Difference between revisions)
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<StructureSection load='6aei' size='340' side='right'caption='[[6aei]], [[Resolution|resolution]] 2.89Å' scene=''> | <StructureSection load='6aei' size='340' side='right'caption='[[6aei]], [[Resolution|resolution]] 2.89Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6aei]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AEI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AEI FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6aei]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AEI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AEI FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LPP:2-(HEXADECANOYLOXY)-1-[(PHOSPHONOOXY)METHYL]ETHYL+HEXADECANOATE'>LPP</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=Y01:CHOLESTEROL+HEMISUCCINATE'>Y01</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LPP:2-(HEXADECANOYLOXY)-1-[(PHOSPHONOOXY)METHYL]ETHYL+HEXADECANOATE'>LPP</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=Y01:CHOLESTEROL+HEMISUCCINATE'>Y01</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Trpc5, Trp5, Trrp5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=6aei FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6aei OCA], [http://pdbe.org/6aei PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6aei RCSB], [http://www.ebi.ac.uk/pdbsum/6aei PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6aei ProSAT]</span></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=6aei FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6aei OCA], [http://pdbe.org/6aei PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6aei RCSB], [http://www.ebi.ac.uk/pdbsum/6aei PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6aei ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/TRPC5_MOUSE TRPC5_MOUSE]] Thought to form a receptor-activated non-selective calcium permeant cation channel. Probably is operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. Has also been shown to be calcium-selective. May also be activated by intracellular calcium store depletion. | [[http://www.uniprot.org/uniprot/TRPC5_MOUSE TRPC5_MOUSE]] Thought to form a receptor-activated non-selective calcium permeant cation channel. Probably is operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. Has also been shown to be calcium-selective. May also be activated by intracellular calcium store depletion. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The transient receptor potential canonical subfamily member 5 (TRPC5), one of seven mammalian TRPC members, is a nonselective calcium-permeant cation channel. TRPC5 is of considerable interest as a drug target in the treatment of progressive kidney disease, depression, and anxiety. Here, we present the 2.8-A resolution cryo-electron microscopy (cryo-EM) structure of the mouse TRPC5 (mTRPC5) homotetramer. Comparison of the TRPC5 structure to previously determined structures of other TRPC and TRP channels reveals differences in the extracellular pore domain and in the length of the S3 helix. The disulfide bond at the extracellular side of the pore and a preceding small loop are essential elements for its proper function. This high-resolution structure of mTRPC5, combined with electrophysiology and mutagenesis, provides insight into the lipid modulation and gating mechanisms of the TRPC family of ion channels. | ||
| + | |||
| + | Cryo-EM structure of TRPC5 at 2.8-A resolution reveals unique and conserved structural elements essential for channel function.,Duan J, Li J, Chen GL, Ge Y, Liu J, Xie K, Peng X, Zhou W, Zhong J, Zhang Y, Xu J, Xue C, Liang B, Zhu L, Liu W, Zhang C, Tian XL, Wang J, Clapham DE, Zeng B, Li Z, Zhang J Sci Adv. 2019 Jul 24;5(7):eaaw7935. doi: 10.1126/sciadv.aaw7935. eCollection 2019, Jul. PMID:31355338<ref>PMID:31355338</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6aei" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| + | [[Category: Lk3 transgenic mice]] | ||
[[Category: Duan, J]] | [[Category: Duan, J]] | ||
[[Category: Li, J]] | [[Category: Li, J]] | ||
Revision as of 17:16, 14 August 2019
Cryo-EM structure of the receptor-activated TRPC5 ion channel
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Categories: Large Structures | Lk3 transgenic mice | Duan, J | Li, J | Li, Z | Zhang, J | Cryo-em | Ion channel | Membrane protein | Mouse trpc5
