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6nq2

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'''Unreleased structure'''
 
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The entry 6nq2 is ON HOLD until Paper Publication
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==Cryo-EM structure of human TPC2 channel in the ligand-bound closed state==
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<StructureSection load='6nq2' size='340' side='right'caption='[[6nq2]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6nq2]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NQ2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6NQ2 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EUJ:(2R)-3-{[(S)-hydroxy{[(1S,2R,3R,4S,5S,6R)-2,4,6-trihydroxy-3,5-bis(phosphonooxy)cyclohexyl]oxy}phosphoryl]oxy}propane-1,2-diyl+dioctanoate'>EUJ</scene></td></tr>
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<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=6nq2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nq2 OCA], [http://pdbe.org/6nq2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6nq2 RCSB], [http://www.ebi.ac.uk/pdbsum/6nq2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6nq2 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors:
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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>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 6nq2" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Bai, X]]
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[[Category: Chen, Q]]
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[[Category: Guo, J]]
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[[Category: Jiang, Y]]
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[[Category: She, J]]
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[[Category: Zeng, W]]
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[[Category: Channel]]
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[[Category: Lysosome]]
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[[Category: Transport protein]]

Revision as of 06:45, 27 March 2019

Cryo-EM structure of human TPC2 channel in the ligand-bound closed state

PDB ID 6nq2

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