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BMKTX TOXIN FROM SCORPION BUTHUS MARTENSII KARSCH, NMR, 25 STRUCTURES
Structural highlights
FunctionKAX36_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.[1] [2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedBmKTX 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[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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