View source for 1dem


==PROTEINASE INHIBITOR HOMOLOGUES AS POTASSIUM CHANNEL BLOCKERS==
<StructureSection load='1dem' size='340' side='right'caption='[[1dem]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1dem]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Dendroaspis_polylepis_polylepis Dendroaspis polylepis polylepis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DEM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DEM FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 1 model</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=1dem FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dem OCA], [https://pdbe.org/1dem PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dem RCSB], [https://www.ebi.ac.uk/pdbsum/1dem PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dem ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/VKTH1_DENPO VKTH1_DENPO] Serine protease inhibitor homolog that blocks voltage-gated potassium channels (Kv1.1/KCNA1, Kv1.2/KCNA2, and Kv1.6/KCNA6) (IC(50)=0.13-50 nM).<ref>PMID:8612784</ref> 
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/de/1dem_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1dem ConSurf].
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== Publication Abstract from PubMed ==
We report here the NMR structure of dendrotoxin I, a powerful potassium channel blocker from the venom of the African Elapidae snake Dendroaspis polylepis polylepis (black mamba), calculated from an experimentally-derived set of 719 geometric restraints. The backbone of the toxin superimposes on bovine pancreatic trypsin inhibitor (BPTI) with a root-mean-square deviation of &lt; 1.7 A. The surface electrostatic potential calculated for dendrotoxin I and BPTI, reveal an important difference which might account for the differences in function of the two proteins. These proteins may provide examples of adaptation for specific and diverse biological functions while at the same time maintaining the overall three-dimensional structure of a common ancestor.

Proteinase inhibitor homologues as potassium channel blockers.,Lancelin JM, Foray MF, Poncin M, Hollecker M, Marion D Nat Struct Biol. 1994 Apr;1(4):246-50. PMID:7544683<ref>PMID:7544683</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
*[[Dendrotoxin|Dendrotoxin]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Dendroaspis polylepis polylepis]]
[[Category: Large Structures]]
[[Category: Foray M-F]]
[[Category: Lancelin J-M]]