6djr

<table><tr><td colspan='2'>[[6djr]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DJR OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6DJR FirstGlance]. <br>

</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6djr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6djr OCA], [http://pdbe.org/6djr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6djr RCSB], [http://www.ebi.ac.uk/pdbsum/6djr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6djr ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

The transient receptor potential ion channels support Ca(2+) permeation in many organs, including the heart, brain, and kidney. Genetic mutations in transient receptor potential cation channel subfamily C member 3 (TRPC3) are associated with neurodegenerative diseases, memory loss, and hypertension. To better understand the conformational changes that regulate TRPC3 function, we solved the cryo-EM structures for the full-length human TRPC3 and its cytoplasmic domain (CPD) in the apo state at 5.8 and 4.0 A resolution, respectively. These structures revealed that the TRPC3 transmembrane domain resembles those of other TRP channels and that the CPD is a stable module involved in channel assembly and gating. We observed the presence of a C-terminal domain swap at the center of the CPD, where horizontal helices (HHs) transition into a coiled-coil bundle. Comparison of TRPC3 structures revealed that the HHs can reside in two distinct positions. Electrophysiological analyses disclosed that shortening the length of the C-terminal loop connecting the HH with the TRP helices increases TRPC3 activity and that elongating the length of the loop has the opposite effect. Our findings indicate that the C-terminal loop affects channel gating by altering the allosteric coupling between the cytoplasmic and transmembrane domains. We propose that molecules that target the HH may represent a promising strategy for controlling TRPC3-associated neurological disorders and hypertension.

Structure-function analyses of the ion channel TRPC3 reveal that its cytoplasmic domain allosterically modulates channel gating.,Sierra-Valdez F, Azumaya CM, Romero LO, Nakagawa T, Cordero-Morales JF J Biol Chem. 2018 Aug 23. pii: RA118.005066. doi: 10.1074/jbc.RA118.005066. PMID:30139744<ref>PMID:30139744</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 6djr" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Human]]

[[Category: Azumaya, C M]]

[[Category: Cordero-Morales, J F]]

[[Category: Nakagawa, T]]

[[Category: Sierra-Valdez, F J]]

[[Category: Trp channel]]