5v02

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'''Unreleased structure'''
 
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The entry 5v02 is ON HOLD until Paper Publication
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==A positive allosteric modulator binding pocket in SK2 ion channels is shared by Riluzole and CyPPA==
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<StructureSection load='5v02' size='340' side='right' caption='[[5v02]], [[Resolution|resolution]] 1.78&Aring;' scene=''>
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Authors: Liu, S.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5v02]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5V02 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5V02 FirstGlance]. <br>
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Description: A positive allosteric modulator binding pocket in SK2 ion channels is shared by Riluzole and CyPPA
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=657:6-(trifluoromethoxy)-1,3-benzothiazol-2-amine'>657</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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[[Category: Unreleased Structures]]
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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=5v02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v02 OCA], [http://pdbe.org/5v02 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5v02 RCSB], [http://www.ebi.ac.uk/pdbsum/5v02 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5v02 ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[[http://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.
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== Function ==
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[[http://www.uniprot.org/uniprot/KCNN2_HUMAN KCNN2_HUMAN]] Forms a voltage-independent potassium channel activated by intracellular calcium. Activation is followed by membrane hyperpolarization. Thought to regulate neuronal excitability by contributing to the slow component of synaptic afterhyperpolarization. The channel is blocked by apamin. [[http://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>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Liu, S]]
[[Category: Liu, S]]
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[[Category: Activator]]
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[[Category: Calcium-activated ion channel]]
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[[Category: Calmodulin]]
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[[Category: Transport protein-metal binding protein complex]]

Revision as of 05:01, 8 March 2018

A positive allosteric modulator binding pocket in SK2 ion channels is shared by Riluzole and CyPPA

5v02, resolution 1.78Å

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