2n7g

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m (Protected "2n7g" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 2n7g is ON HOLD until Paper Publication
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==Structure of the cyclic nucleotide-binding homology domain of the hERG channel==
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<StructureSection load='2n7g' size='340' side='right' caption='[[2n7g]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2n7g]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N7G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2N7G FirstGlance]. <br>
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</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=2n7g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n7g OCA], [http://pdbe.org/2n7g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2n7g RCSB], [http://www.ebi.ac.uk/pdbsum/2n7g PDBsum]</span></td></tr>
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</table>
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== Disease ==
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[[http://www.uniprot.org/uniprot/KCNH2_HUMAN KCNH2_HUMAN]] Defects in KCNH2 are the cause of long QT syndrome type 2 (LQT2) [MIM:[http://omim.org/entry/613688 613688]]. 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. Deafness is often associated with LQT2.<ref>PMID:16361248</ref> <ref>PMID:9600240</ref> <ref>PMID:7889573</ref> <ref>PMID:8914737</ref> <ref>PMID:8635257</ref> <ref>PMID:8877771</ref> <ref>PMID:9024139</ref> <ref>PMID:9693036</ref> <ref>PMID:9544837</ref> <ref>PMID:9452080</ref> <ref>PMID:10086971</ref> <ref>PMID:10220144</ref> <ref>PMID:10187793</ref> <ref>PMID:10517660</ref> <ref>PMID:10735633</ref> <ref>PMID:10973849</ref> <ref>PMID:10862094</ref> <ref>PMID:10753933</ref> <ref>PMID:12062363</ref> <ref>PMID:12354768</ref> <ref>PMID:12621127</ref> <ref>PMID:15051636</ref> <ref>PMID:15840476</ref> <ref>PMID:22314138</ref> Defects in KCNH2 are the cause of short QT syndrome type 1 (SQT1) [MIM:[http://omim.org/entry/609620 609620]]. 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:14676148</ref> <ref>PMID:15828882</ref>
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== Function ==
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[[http://www.uniprot.org/uniprot/KCNH2_HUMAN KCNH2_HUMAN]] Pore-forming (alpha) subunit of voltage-gated inwardly rectifying potassium channel. Channel properties are modulated by cAMP and subunit assembly. Mediates the rapidly activating component of the delayed rectifying potassium current in heart (IKr). Isoform 3 has no channel activity by itself, but modulates channel characteristics when associated with isoform 1.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The human ether-a-go-go related gene (hERG) channel is crucial for the cardiac action potential by contributing to the fast delayed-rectifier potassium current. Mutations in the hERG channel result in type 2 long QT syndrome (LQT2). The hERG channel contains a cyclic nucleotide-binding homology domain (CNBHD) and this domain is required for the channel gating though molecular interactions with the eag domain. Here we present solution structure of the CNBHD of the hERG channel. The structural study reveals that the CNBHD adopts a similar fold to other KCNH channels. It is self-liganded and it contains a short beta-strand that blocks the nucleotide-binding pocket in the beta-roll. Folding of LQT2-related mutations in this domain was shown to be affected by point mutation. Mutations in this domain can cause protein aggregation in E. coli cells or induce conformational changes. One mutant-R752W showed obvious chemical shift perturbation compared with the wild-type, but it still binds to the eag domain. The helix region from the N-terminal cap domain of the hERG channel showed unspecific interactions with the CNBHD.
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Authors: Li, Y., Ng, H., Li, Q., Kang, C.
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Structure of the Cyclic Nucleotide-Binding Homology Domain of the hERG Channel and Its Insight into Type 2 Long QT Syndrome.,Li Y, Ng HQ, Li Q, Kang C Sci Rep. 2016 Mar 30;6:23712. doi: 10.1038/srep23712. PMID:27025590<ref>PMID:27025590</ref>
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Description: Structure of the cyclic nucleotide-binding homology domain of the hERG channel
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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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[[Category: Ng, H]]
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<div class="pdbe-citations 2n7g" 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>
[[Category: Kang, C]]
[[Category: Kang, C]]
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[[Category: Li, Y]]
 
[[Category: Li, Q]]
[[Category: Li, Q]]
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[[Category: Li, Y]]
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[[Category: Ng, H]]
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[[Category: Cnbhd]]
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[[Category: Herg]]
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[[Category: Ion channel]]
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[[Category: Lqts2]]
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[[Category: Membrane protein]]

Revision as of 15:46, 1 June 2016

Structure of the cyclic nucleotide-binding homology domain of the hERG channel

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