8sim - Revision history

OCA at 06:58, 19 June 2024

2024-06-19T06:58:46Z

← Older revision		Revision as of 06:58, 19 June 2024
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[8sim]] 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=8SIM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8SIM FirstGlance]. <br>		<table><tr><td colspan='2'>[[8sim]] 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=8SIM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8SIM FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>		</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution\|Resolution]] 6.2Å</td></tr>
			<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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=8sim FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8sim OCA], [https://pdbe.org/8sim PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8sim RCSB], [https://www.ebi.ac.uk/pdbsum/8sim PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8sim ProSAT]</span></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=8sim FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8sim OCA], [https://pdbe.org/8sim PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8sim RCSB], [https://www.ebi.ac.uk/pdbsum/8sim PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8sim ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
	[https://www.uniprot.org/uniprot/~~KCNQ1_HUMAN KCNQ1_HUMAN~~] Defects in KCNQ1 are the cause of long QT syndrome type 1 (LQT1) [MIM:[https://omim.org/entry/192500 192500]; also known as Romano-Ward syndrome (RWS). Long QT syndromes are heart disorders characterized by ~~a prolonged QT interval on~~ the ~~ECG and polymorphic ventricular arrhythmias. They cause syncope and sudden death~~ in ~~response to exercise or emotional stress~~. LQT1 inheritance is an autosomal dominant.<ref>PMID:18165683</ref> <ref>PMID:9799083</ref> <ref>PMID:10024302</ref> <ref>PMID:8528244</ref> <ref>PMID:9323054</ref> <ref>PMID:8872472</ref> <ref>PMID:8818942</ref> [:]<ref>PMID:9024139</ref> <ref>PMID:9386136</ref> <ref>PMID:9272155</ref> <ref>PMID:9302275</ref> <ref>PMID:9570196</ref> <ref>PMID:9641694</ref> <ref>PMID:9693036</ref> <ref>PMID:9482580</ref> <ref>PMID:9702906</ref> <ref>PMID:10367071</ref> <ref>PMID:9927399</ref> <ref>PMID:10482963</ref> <ref>PMID:10220144</ref> <ref>PMID:10220146</ref> <ref>PMID:10409658</ref> <ref>PMID:10728423</ref> <ref>PMID:10973849</ref> <ref>PMID:15840476</ref> <ref>PMID:19540844</ref> <ref>PMID:21241800</ref> Defects in ~~KCNQ1~~ are the cause of ~~Jervell and Lange-Nielsen syndrome type 1 (JLNS1) [MIM:[https://omim~~.~~org/entry/220400 220400]. JLNS1~~ is ~~an autosomal recessive disorder characterized~~ by ~~congenital deafness, prolongation of~~ the ~~QT interval, syncopal attacks due to ventricular arrhythmias, and a high risk of sudden death.<ref>PMID:10728423</ref> <ref>PMID:9781056</ref> <ref>PMID:10090886</ref> Defects~~ in ~~KCNQ1 are the cause of familial atrial fibrillation type 3 (ATFB3) [MIM:[https://omim.org/~~entry/607554 607554]. Atrial fibrillation is a common disorder of cardiac rhythm that is hereditary in a small subgroup of patients. It is characterized by disorganized atrial electrical activity and ineffective atrial contraction promoting blood stasis in the atria and reduces ventricular filling. It can result in palpitations, syncope, thromboembolic stroke, and congestive heart failure.~~<ref>PMID:12522251</ref> Defects~~ in ~~KCNQ1~~ are the cause of short QT syndrome type 2 (SQT2) [MIM:[https://omim.org/entry/609621 609621]. Short QT syndromes are heart disorders characterized by idiopathic persistently and uniformly short QT interval on ECG in the absence of structural heart disease in affected individuals. They cause syncope and sudden death.~~<ref>PMID:15159330</ref>~~		[https://www.uniprot.org/uniprot/CALM1_HUMAN CALM1_HUMAN] The disease is caused by mutations affecting the gene represented in this entry. Mutations in CALM1 are the cause of CPVT4. The disease is caused by mutations affecting the gene represented in this entry. Mutations in CALM1 are the cause of LQT14.
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/~~KCNQ1_HUMAN KCNQ1_HUMAN~~] ~~Probably important in cardiac repolarization. Associates with KCNE1 (MinK) to form~~ the ~~I(Ks) cardiac potassium current. Elicits~~ a rapidly activating, potassium-selective outward current. Muscarinic agonist oxotremorine-M strongly suppresses KCNQ1/KCNE1 current in CHO cells in which cloned KCNQ1/KCNE1 channels were coexpressed with M1 muscarinic receptors. May associate also with KCNE3 (MiRP2) to form the potassium channel that is important for cyclic AMP-stimulated intestinal secretion of ~~chloride ions~~, ~~which is reduced in cystic fibrosis and pathologically stimulated in cholera and other forms of secretory diarrhea.~~		[https://www.uniprot.org/uniprot/CALM1_HUMAN CALM1_HUMAN] Calmodulin mediates the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis (PubMed:16760425). Mediates calcium-dependent inactivation of CACNA1C (PubMed:26969752). Positively regulates calcium-activated potassium channel activity of KCNN2 (PubMed:27165696).<ref>PMID:16760425</ref> <ref>PMID:23893133</ref> <ref>PMID:26969752</ref> <ref>PMID:27165696</ref>
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	~~Voltage-dependent~~ ion channels ~~underlie the propagation of action potentials~~ and other ~~forms of electrical activity in cells. In these~~ proteins~~, voltage sensor domains (VSDs) regulate opening and closing of the pore~~ through ~~the displacement of their positive~~-~~charged S4 helix in response to~~ the ~~membrane voltage. The movement of S4 at hyperpolarizing membrane voltages in some channels is thought~~ to ~~directly clamp the pore shut through the S4-S5 linker helix. The KCNQ1 channel (also known as K(v)7.1), which is important for heart rhythm, is regulated not only by membrane voltage but also~~ by the ~~signaling lipid phosphatidylinositol 4,5~~-~~bisphosphate (PIP(2)). KCNQ1 requires PIP(2) to open~~ and ~~to couple the movement of S4 in the VSD to the pore~~. ~~To understand the mechanism of this voltage regulation, we use cryogenic electron microscopy to visualize the movement of S4 in the human KCNQ1 channel in lipid membrane vesicles~~ with ~~a voltage difference across the membrane~~, ~~i.e., an applied electric field~~ in ~~the membrane. Hyperpolarizing voltages displace S4 in such~~ a ~~manner as to sterically occlude~~ the ~~PIP~~(2)-~~binding site. Thus, in KCNQ1, the voltage sensor acts primarily as a regulator~~ of ~~PIP~~(2) ~~binding~~. ~~The voltage sensors' influence on the~~ channel~~'s gate is indirect through the reaction sequence~~: ~~voltage sensor movement --> alter PIP(2~~) ~~ligand affinity --> alter pore opening~~.

	The membrane electric field regulates the PIP(2)-binding site to gate the KCNQ1 channel.,Mandala VS, MacKinnon R Proc Natl Acad Sci U S A. 2023 May 23;120(21):e2301985120. doi: , 10.1073/pnas.2301985120. Epub 2023 May 16. PMID:37192161<ref>PMID:37192161</ref>		==See Also==
			*[[Potassium channel 3D structures\|Potassium channel 3D structures]]
	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class~~=~~"pdbe-citations 8sim" style~~=~~"background-color:#fffaf0;"></div>~~
	== References ==		== References ==
	<references/>		<references/>

OCA at 05:47, 31 May 2023

2023-05-31T05:47:15Z

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-The entry 8sim is ON HOLD
+==KCNQ1 with voltage sensor in the intermediate conformation==
-Authors:
+The membrane electric field regulates the PIP(2)-binding site to gate the KCNQ1 channel.,Mandala VS, MacKinnon R Proc Natl Acad Sci U S A. 2023 May 23;120(21):e2301985120. doi: , 10.1073/pnas.2301985120. Epub 2023 May 16. PMID:37192161<ref>PMID:37192161</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>

OCA: Protected "8sim" [edit=sysop:move=sysop]

2023-04-26T15:26:03Z

Protected "8sim" [edit=sysop:move=sysop]

← Older revision	Revision as of 15:26, 26 April 2023
(No difference)

OCA: New page: '''Unreleased structure''' The entry 8sim is ON HOLD Authors: Description: Category: Unreleased Structures

2023-04-26T15:26:02Z

New page: '''Unreleased structure''' The entry 8sim is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 8sim is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]