1den

<StructureSection load='1den' size='340' side='right' caption='[[1den]], [[NMR_Ensembles_of_Models | 29 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1den]] is a 1 chain structure with sequence from [http://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=1DEN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DEN FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1dem|1dem]]</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=1den FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1den OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1den RCSB], [http://www.ebi.ac.uk/pdbsum/1den PDBsum]</span></td></tr>

[[http://www.uniprot.org/uniprot/IVBII_DENPO IVBII_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).

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/de/1den_consurf.spt"</scriptWhenChecked>

</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/chain_selection.php?pdb_ID=2ata 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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[[Category: Foray, M F]]

[[Category: Lancelin, J M]]