6nq1: Difference between revisions
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The | ==Cryo-EM structure of human TPC2 channel in the apo state== | ||
<SX load='6nq1' size='340' side='right' viewer='molstar' caption='[[6nq1]], [[Resolution|resolution]] 3.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6nq1]] is a 2 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=6NQ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6NQ1 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.5Å</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=6nq1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nq1 OCA], [https://pdbe.org/6nq1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6nq1 RCSB], [https://www.ebi.ac.uk/pdbsum/6nq1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6nq1 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/TPC2_HUMAN TPC2_HUMAN] Nicotinic acid adenine dinucleotide phosphate (NAADP) receptor that may function as one of the major voltage-gated Ca(2+) channels (VDCC) across the lysosomal membrane. May be involved in smooth muscle contraction.<ref>PMID:19387438</ref> <ref>PMID:19620632</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Mammalian two-pore channels (TPCs) regulate the physiological functions of the endolysosome. Here we present cryo-EM structures of human TPC2 (HsTPC2), a phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2)-activated, Na(+) selective channel, in the ligand-bound and apo states. The apo structure captures the closed conformation, while the ligand-bound form features the channel in both open and closed conformations. Combined with functional analysis, these structures provide insights into the mechanism of PI(3,5)P2-regulated gating of TPC2, which is distinct from that of TPC1. Specifically, the endolysosome-specific PI(3,5)P2 binds at the first 6-TM and activates the channel - independently of the membrane potential - by inducing a structural change at the pore-lining inner helix (IS6), which forms a continuous helix in the open state but breaks into two segments at Gly317 in the closed state. Additionally, structural comparison to the voltage-dependent TPC1 structure allowed us to identify Ile551 as being responsible for the loss of voltage dependence in TPC2. | |||
Structural mechanisms of phospholipid activation of the human TPC2 channel.,She J, Zeng W, Guo J, Chen Q, Bai XC, Jiang Y Elife. 2019 Mar 12;8. pii: 45222. doi: 10.7554/eLife.45222. PMID:30860481<ref>PMID:30860481</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6nq1" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Ion channels 3D structures|Ion channels 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</SX> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Bai X]] | |||
[[Category: Chen Q]] | |||
[[Category: Guo J]] | |||
[[Category: Jiang Y]] | |||
[[Category: She J]] | |||
[[Category: Zeng W]] | |||
Latest revision as of 12:55, 6 November 2024
Cryo-EM structure of human TPC2 channel in the apo state
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