6cud
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | The entry | + | ==Structure of the human TRPC3 in a lipid-occupied, closed state== |
| - | + | <StructureSection load='6cud' size='340' side='right' caption='[[6cud]], [[Resolution|resolution]] 3.30Å' scene=''> | |
| - | + | == 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 [http://oca.weizmann.ac.il/oca-docs/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:(2R)-3-hydroxypropane-1,2-diyl+dihexanoate'>FGJ</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | |
| - | [[Category: | + | <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=6cud FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cud OCA], [http://pdbe.org/6cud PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cud RCSB], [http://www.ebi.ac.uk/pdbsum/6cud PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cud ProSAT]</span></td></tr> |
| + | </table> | ||
| + | == Disease == | ||
| + | [[http://www.uniprot.org/uniprot/TRPC3_HUMAN TRPC3_HUMAN]] The disease is caused by mutations affecting the gene represented in this entry. | ||
| + | == Function == | ||
| + | [[http://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> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Choi, W]] | ||
| + | [[Category: Du, J]] | ||
| + | [[Category: Fan, C]] | ||
| + | [[Category: Lu, W]] | ||
| + | [[Category: Membrane protein]] | ||
Revision as of 05:32, 16 May 2018
Structure of the human TRPC3 in a lipid-occupied, closed state
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Categories: Choi, W | Du, J | Fan, C | Lu, W | Membrane protein
