1bkt

<StructureSection load='1bkt' size='340' side='right' caption='[[1bkt]], [[NMR_Ensembles_of_Models | 25 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1bkt]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buthus_martensi Buthus martensi]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BKT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BKT FirstGlance]. <br>

</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></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=1bkt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bkt OCA], [http://pdbe.org/1bkt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bkt RCSB], [http://www.ebi.ac.uk/pdbsum/1bkt PDBsum]</span></td></tr>

[[http://www.uniprot.org/uniprot/KAX36_MESMA KAX36_MESMA]] Blocks voltage-gated potassium channels. At 2 uM, blocks rat Kv1.1/KCNA1 and Kv1.3/KCNA3, has a strong effect on rat Kv1.2/KCNA2 and Kv1.6/KCNA6 as well as a moderate effect on Shaker IR.<ref>PMID:9354615</ref> <ref>PMID:20713119</ref>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bk/1bkt_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].

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

BmKTX is a toxin recently purified from the venom of Buthus Martensi, which belongs to the kaliotoxin family. We have determined its solution structure by use of conventional two-dimensional NMR techniques followed by distance-geometry and energy minimization. The calculated structure is composed of a short alpha-helix (residues 14 to 20) connected by a tight turn to a two-stranded antiparallel beta-sheet (sequences 25-27 and 32-34). The beta-turn connecting these strands belongs to type I. The N-terminal segment (sequence 1 to 8) runs parallel to the beta-sheet although it cannot be considered as a third strand. Comparison of the conformation of BmKTX and toxins of the kaliotoxin family clearly demonstrates that they are highly related. Therefore, analysis of the residues belonging to the interacting surface of those toxins allows us to propose a functional map of BmKTX slightly different from the one of KTX and AgTX2, which may explain the variations in affinities of these toxins towards the Kv1.3 channels.

Solution structure of BmKTX, a K+ blocker toxin from the Chinese scorpion Buthus Martensi.,Renisio JG, Romi-Lebrun R, Blanc E, Bornet O, Nakajima T, Darbon H Proteins. 2000 Jan 1;38(1):70-8. PMID:10651040<ref>PMID:10651040</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 1bkt" style="background-color:#fffaf0;"></div>

*[[Potassium channel toxin|Potassium channel toxin]]

[[Category: Buthus martensi]]

[[Category: Blanc, E]]

[[Category: Bornet, O]]

[[Category: Darbon, H]]

[[Category: Nakajima, T]]

[[Category: Renisio, J G]]

[[Category: Romi-Lebrun, R]]

[[Category: Voltage gated potassium channel]]