6cud
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==Structure of the human TRPC3 in a lipid-occupied, closed state== | ==Structure of the human TRPC3 in a lipid-occupied, closed state== | ||
| - | < | + | <SX load='6cud' size='340' side='right' viewer='molstar' caption='[[6cud]], [[Resolution|resolution]] 3.30Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6cud]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CUD OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[6cud]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CUD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CUD FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6OE:(2S)-3-{[(S)-(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-2-(HEXANOYLOXY)PROPYL+HEXANOATE'>6OE</scene>, <scene name='pdbligand=FGJ:( | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.3Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6OE:(2S)-3-{[(S)-(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-2-(HEXANOYLOXY)PROPYL+HEXANOATE'>6OE</scene>, <scene name='pdbligand=FGJ:[(2~{R})-2-hexanoyloxy-3-oxidanyl-propyl]+hexanoate'>FGJ</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=6cud FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cud OCA], [https://pdbe.org/6cud PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6cud RCSB], [https://www.ebi.ac.uk/pdbsum/6cud PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6cud ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Disease == | == Disease == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/TRPC3_HUMAN TRPC3_HUMAN] The disease is caused by mutations affecting the gene represented in this entry. |
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/TRPC3_HUMAN TRPC3_HUMAN] 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. Activated by diacylglycerol (DAG) in a membrane-delimited fashion, independently of protein kinase C, and by inositol 1,4,5-triphosphate receptors (ITPR) with bound IP3. May also be activated by internal calcium store depletion.<ref>PMID:20095964</ref> <ref>PMID:8646775</ref> <ref>PMID:9417057</ref> <ref>PMID:9930701</ref> |
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The TRPC channels are crucially involved in store-operated calcium entry and calcium homeostasis, and they are implicated in human diseases such as neurodegenerative disease, cardiac hypertrophy, and spinocerebellar ataxia. We present a structure of the full-length human TRPC3, a lipid-gated TRPC member, in a lipid-occupied, closed state at 3.3 Angstrom. TRPC3 has four elbow-like membrane reentrant helices prior to the first transmembrane helix. The TRP helix is perpendicular to, and thus disengaged from, the pore-lining S6, suggesting a different gating mechanism from other TRP subfamily channels. The third transmembrane helix S3 is remarkably long, shaping a unique transmembrane domain, and constituting an extracellular domain that may serve as a sensor of external stimuli. We identified two lipid binding sites, one being sandwiched between the pre-S1 elbow and the S4-S5 linker, and the other being close to the ion-conducting pore, where the conserved LWF motif of the TRPC family is located. | ||
| + | |||
| + | Structure of the human lipid-gated cation channel TRPC3.,Fan C, Choi W, Sun W, Du J, Lu W Elife. 2018 May 4;7. pii: 36852. doi: 10.7554/eLife.36852. PMID:29726814<ref>PMID:29726814</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6cud" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
| - | </ | + | </SX> |
| - | [[Category: Choi | + | [[Category: Homo sapiens]] |
| - | [[Category: Du | + | [[Category: Large Structures]] |
| - | [[Category: Fan | + | [[Category: Choi W]] |
| - | [[Category: Lu | + | [[Category: Du J]] |
| - | + | [[Category: Fan C]] | |
| + | [[Category: Lu W]] | ||
Current revision
Structure of the human TRPC3 in a lipid-occupied, closed state
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Categories: Homo sapiens | Large Structures | Choi W | Du J | Fan C | Lu W
