5yx9
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | The entry | + | ==Cryo-EM structure of human TRPC6 at 3.8A resolution== |
| + | <StructureSection load='5yx9' size='340' side='right' caption='[[5yx9]], [[Resolution|resolution]] 3.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5yx9]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YX9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YX9 FirstGlance]. <br> | ||
| + | </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=5yx9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yx9 OCA], [http://pdbe.org/5yx9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yx9 RCSB], [http://www.ebi.ac.uk/pdbsum/5yx9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yx9 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Disease == | ||
| + | [[http://www.uniprot.org/uniprot/TRPC6_HUMAN TRPC6_HUMAN]] Familial idiopathic steroid-resistant nephrotic syndrome with focal segmental hyalinosis. The disease is caused by mutations affecting the gene represented in this entry. | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/TRPC6_HUMAN TRPC6_HUMAN]] Thought to form a receptor-activated non-selective calcium permeant cation channel (PubMed:19936226, PubMed:23291369). 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 (PubMed:26892346). Seems not to be activated by intracellular calcium store depletion.<ref>PMID:19936226</ref> <ref>PMID:23291369</ref> <ref>PMID:26892346</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | TRPC6 and TRPC3 are receptor-activated nonselective cation channels that belong to the family of canonical transient receptor potential (TRPC) channels. They are activated by diacylglycerol, a lipid second messenger. TRPC6 and TRPC3 are involved in many physiological processes and implicated in human genetic diseases. Here we present the structure of human TRPC6 homotetramer in complex with a newly identified high-affinity inhibitor BTDM solved by single-particle cryo-electron microscopy to 3.8 A resolution. We also present the structure of human TRPC3 at 4.4 A resolution. These structures show two-layer architectures in which the bell-shaped cytosolic layer holds the transmembrane layer. Extensive inter-subunit interactions of cytosolic domains, including the N-terminal ankyrin repeats and the C-terminal coiled-coil, contribute to the tetramer assembly. The high-affinity inhibitor BTDM wedges between the S5-S6 pore domain and voltage sensor-like domain to inhibit channel opening. Our structures uncover the molecular architecture of TRPC channels and provide a structural basis for understanding the mechanism of these channels. | ||
| - | + | Structure of the receptor-activated human TRPC6 and TRPC3 ion channels.,Tang Q, Guo W, Zheng L, Wu JX, Liu M, Zhou X, Zhang X, Chen L Cell Res. 2018 Apr 26. pii: 10.1038/s41422-018-0038-2. doi:, 10.1038/s41422-018-0038-2. PMID:29700422<ref>PMID:29700422</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5yx9" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Chen, L]] | ||
| + | [[Category: Guo, W]] | ||
| + | [[Category: Tang, Q]] | ||
| + | [[Category: Membrane protein]] | ||
| + | [[Category: Trpc6 channel]] | ||
Revision as of 07:18, 23 May 2018
Cryo-EM structure of human TRPC6 at 3.8A resolution
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