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1ne5

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{{Seed}}
 
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[[Image:1ne5.png|left|200px]]
 
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==Solution Structure of HERG Specific Scorpion Toxin CnErg1==
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The line below this paragraph, containing "STRUCTURE_1ne5", creates the "Structure Box" on the page.
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<StructureSection load='1ne5' size='340' side='right'caption='[[1ne5]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1ne5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Centruroides_noxius Centruroides noxius]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NE5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NE5 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ne5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ne5 OCA], [https://pdbe.org/1ne5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ne5 RCSB], [https://www.ebi.ac.uk/pdbsum/1ne5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ne5 ProSAT]</span></td></tr>
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{{STRUCTURE_1ne5| PDB=1ne5 | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/KGX11_CENNO KGX11_CENNO] Blocks human and rat Kv11.1/KCNH2/ERG1 and Kv11.3/KCNH7/ERG3, as well as rat (but not human) Kv11.2/KCNH6/ERG2 (PubMed:11755529, PubMed:11864985, PubMed:16497878, PubMed:17369411, PubMed:20600425) by binding to channel outer vestibule (S5P domain) with a 1:1 stoichiometry (PubMed:11755529, PubMed:11864985, PubMed:17369411, PubMed:20600425). Inhibition data are the following: hERG1 (reversible, IC(50)~7 nM) (PubMed:11755529, PubMed:11864985, PubMed:16497878, PubMed:17369411, PubMed:20600425), rERG1 (reversible, Kd=6.8 nM) (PubMed:16497878), rERG2 (irreversible, Kd=2.8 nM) (PubMed:16497878), hERG3 (irreversible, Kd=4.05 nM) (PubMed:16497878) and rERG3 (reversible, Kd=38.1 nM) (PubMed:16497878) potassium channels. The toxin potency is not affected by elevating potassium ion concentration from 2 to 98 mM (PubMed:11864985). This toxin only blocks channels in a closed state (PubMed:12860380). At high toxin concentrations, block of Kv11.1/KCNH2/ERG1 macroscopic current is incomplete (93.5%). This suggests a kinetic mechanism model with two different states of toxin-channel binding (T+C=TC*=TC; in the TC* state, the toxin binds the channel but does not occlude the pore, whereas in the TC state the toxin binds and occludes the pore). In this model, incomplete block is explained by the relatively fast dissociation rate from the blocked channel conformation (TC) relative to the rate of conversion of the toxin-channel encounter complex (TC*) to the blocked channel conformation (TC) (PubMed:17369411).<ref>PMID:10224238</ref> <ref>PMID:11755529</ref> <ref>PMID:11864985</ref> <ref>PMID:12860380</ref> <ref>PMID:16497878</ref> <ref>PMID:17369411</ref> <ref>PMID:20600425</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ne/1ne5_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ne5 ConSurf].
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<div style="clear:both"></div>
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===Solution Structure of HERG Specific Scorpion Toxin CnErg1===
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==See Also==
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*[[Potassium channel toxin 3D structures|Potassium channel toxin 3D structures]]
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== References ==
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<references/>
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The line below this paragraph, {{ABSTRACT_PUBMED_12650941}}, adds the Publication Abstract to the page
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__TOC__
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(as it appears on PubMed at http://www.pubmed.gov), where 12650941 is the PubMed ID number.
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</StructureSection>
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[[Category: Centruroides noxius]]
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{{ABSTRACT_PUBMED_12650941}}
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[[Category: Large Structures]]
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[[Category: Alewood P]]
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==About this Structure==
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[[Category: Kuchel PW]]
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1NE5 is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NE5 OCA].
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[[Category: Paramjit B]]
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[[Category: Torres AM]]
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==Reference==
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[[Category: Vandenberg JI]]
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<ref group="xtra">PMID:12650941</ref><references group="xtra"/>
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[[Category: Alewood, P.]]
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[[Category: Kuchel, P W.]]
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[[Category: Paramjit, B.]]
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[[Category: Torres, A M.]]
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[[Category: Vandenberg, J I.]]
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[[Category: Alpha-helix]]
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[[Category: Toxin]]
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[[Category: Triple-stranded beta-sheet]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Nov 18 20:28:41 2009''
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Current revision

Solution Structure of HERG Specific Scorpion Toxin CnErg1

PDB ID 1ne5

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