9lj1: Difference between revisions

Latest revision as of 11:31, 16 April 2025

Human KCNQ5-CaM-PIP2-HN37 complex in a closed conformation.

Structural highlights

9lj1 is a 8 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 3.2Å
Ligands:	9MF, PIO
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

KCNQ5_HUMAN The disease is caused by mutations affecting the gene represented in this entry.

Function

KCNQ5_HUMAN Associates with KCNQ3 to form a potassium channel which contributes to M-type current, a slowly activating and deactivating potassium conductance which plays a critical role in determining the subthreshold electrical excitability of neurons. Therefore, it is important in the regulation of neuronal excitability. May contribute, with other potassium channels, to the molecular diversity of a heterogeneous population of M-channels, varying in kinetic and pharmacological properties, which underlie this physiologically important current. Insensitive to tetraethylammonium, but inhibited by barium, linopirdine and XE991. Activated by niflumic acid and the anticonvulsant retigabine. As the native M-channel, the potassium channel composed of KCNQ3 and KCNQ5 is also suppressed by activation of the muscarinic acetylcholine receptor CHRM1.^[1] ^[2] ^[3]

References

↑ Lerche C, Scherer CR, Seebohm G, Derst C, Wei AD, Busch AE, Steinmeyer K. Molecular cloning and functional expression of KCNQ5, a potassium channel subunit that may contribute to neuronal M-current diversity. J Biol Chem. 2000 Jul 21;275(29):22395-400. doi: 10.1074/jbc.M002378200. PMID:10787416 doi:https://dx.doi.org/10.1074/jbc.M002378200
↑ Wickenden AD, Zou A, Wagoner PK, Jegla T. Characterization of KCNQ5/Q3 potassium channels expressed in mammalian cells. Br J Pharmacol. 2001 Jan;132(2):381-4. PMID:11159685 doi:https://dx.doi.org/10.1038/sj.bjp.0703861
↑ Lehman A, Thouta S, Mancini GMS, Naidu S, van Slegtenhorst M, McWalter K, Person R, Mwenifumbo J, Salvarinova R, Guella I, McKenzie MB, Datta A, Connolly MB, Kalkhoran SM, Poburko D, Friedman JM, Farrer MJ, Demos M, Desai S, Claydon T. Loss-of-Function and Gain-of-Function Mutations in KCNQ5 Cause Intellectual Disability or Epileptic Encephalopathy. Am J Hum Genet. 2017 Jul 6;101(1):65-74. doi: 10.1016/j.ajhg.2017.05.016. Epub, 2017 Jun 29. PMID:28669405 doi:https://dx.doi.org/10.1016/j.ajhg.2017.05.016

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OCA

[1] Lerche C, Scherer CR, Seebohm G, Derst C, Wei AD, Busch AE, Steinmeyer K. Molecular cloning and functional expression of KCNQ5, a potassium channel subunit that may contribute to neuronal M-current diversity. J Biol Chem. 2000 Jul 21;275(29):22395-400. doi: 10.1074/jbc.M002378200. PMID:10787416 doi:https://dx.doi.org/10.1074/jbc.M002378200

[2] Wickenden AD, Zou A, Wagoner PK, Jegla T. Characterization of KCNQ5/Q3 potassium channels expressed in mammalian cells. Br J Pharmacol. 2001 Jan;132(2):381-4. PMID:11159685 doi:https://dx.doi.org/10.1038/sj.bjp.0703861

[3] Lehman A, Thouta S, Mancini GMS, Naidu S, van Slegtenhorst M, McWalter K, Person R, Mwenifumbo J, Salvarinova R, Guella I, McKenzie MB, Datta A, Connolly MB, Kalkhoran SM, Poburko D, Friedman JM, Farrer MJ, Demos M, Desai S, Claydon T. Loss-of-Function and Gain-of-Function Mutations in KCNQ5 Cause Intellectual Disability or Epileptic Encephalopathy. Am J Hum Genet. 2017 Jul 6;101(1):65-74. doi: 10.1016/j.ajhg.2017.05.016. Epub, 2017 Jun 29. PMID:28669405 doi:https://dx.doi.org/10.1016/j.ajhg.2017.05.016

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[2]

[3]

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-'''Unreleased structure'''
-The entry 9lj1 is ON HOLD  until Paper Publication
+==Human KCNQ5-CaM-PIP2-HN37 complex in a closed conformation.==
+<StructureSection load='9lj1' size='340' side='right'caption='[[9lj1]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
-Authors:
+== Structural highlights ==
+<table><tr><td colspan='2'>[[9lj1]] is a 8 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=9LJ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9LJ1 FirstGlance]. <br>
-Description:
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.2&#8491;</td></tr>
-[[Category: Unreleased Structures]]
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=9MF:methyl+~{N}-[4-[(4-fluorophenyl)methyl-prop-2-ynyl-amino]-2,6-dimethyl-phenyl]carbamate'>9MF</scene>, <scene name='pdbligand=PIO:[(2R)-2-OCTANOYLOXY-3-[OXIDANYL-[(1R,2R,3S,4R,5R,6S)-2,3,6-TRIS(OXIDANYL)-4,5-DIPHOSPHONOOXY-CYCLOHEXYL]OXY-PHOSPHORYL]OXY-PROPYL]+OCTANOATE'>PIO</scene></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=9lj1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9lj1 OCA], [https://pdbe.org/9lj1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9lj1 RCSB], [https://www.ebi.ac.uk/pdbsum/9lj1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9lj1 ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[https://www.uniprot.org/uniprot/KCNQ5_HUMAN KCNQ5_HUMAN] The disease is caused by mutations affecting the gene represented in this entry.
+== Function ==
+[https://www.uniprot.org/uniprot/KCNQ5_HUMAN KCNQ5_HUMAN] Associates with KCNQ3 to form a potassium channel which contributes to M-type current, a slowly activating and deactivating potassium conductance which plays a critical role in determining the subthreshold electrical excitability of neurons. Therefore, it is important in the regulation of neuronal excitability. May contribute, with other potassium channels, to the molecular diversity of a heterogeneous population of M-channels, varying in kinetic and pharmacological properties, which underlie this physiologically important current. Insensitive to tetraethylammonium, but inhibited by barium, linopirdine and XE991. Activated by niflumic acid and the anticonvulsant retigabine. As the native M-channel, the potassium channel composed of KCNQ3 and KCNQ5 is also suppressed by activation of the muscarinic acetylcholine receptor CHRM1.<ref>PMID:10787416</ref> <ref>PMID:11159685</ref> <ref>PMID:28669405</ref>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Guo J]]
+[[Category: Yang Z]]

9lj1: Difference between revisions

Latest revision as of 11:31, 16 April 2025

Human KCNQ5-CaM-PIP2-HN37 complex in a closed conformation.

Structural highlights

Disease

Function

References

Contents

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