6nq1: Difference between revisions
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<StructureSection load='6nq1' size='340' side='right'caption='[[6nq1]], [[Resolution|resolution]] 3.50Å' scene=''> | <StructureSection load='6nq1' size='340' side='right'caption='[[6nq1]], [[Resolution|resolution]] 3.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6nq1]] is a 2 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6NQ1 FirstGlance]. <br> | <table><tr><td colspan='2'>[[6nq1]] is a 2 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=6NQ1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6NQ1 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=6nq1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nq1 OCA], [http://pdbe.org/6nq1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6nq1 RCSB], [http://www.ebi.ac.uk/pdbsum/6nq1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6nq1 ProSAT]</span></td></tr> | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TPCN2, TPC2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=6nq1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nq1 OCA], [http://pdbe.org/6nq1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6nq1 RCSB], [http://www.ebi.ac.uk/pdbsum/6nq1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6nq1 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
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</div> | </div> | ||
<div class="pdbe-citations 6nq1" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6nq1" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Ion channels 3D structures|Ion channels 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Human]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Bai, X]] | [[Category: Bai, X]] | ||
Revision as of 20:37, 20 November 2019
Cryo-EM structure of human TPC2 channel in the apo stateCryo-EM structure of human TPC2 channel in the apo state
Structural highlights
Function[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.[1] [2] Publication Abstract from PubMedMammalian 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[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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