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|Title:||Functional site of bukatoxin, an α-type sodium channel neurotoxin from the Chinese scorpion (Buthus martensi Karsch) venom: Probable role of the52PDKVP56loop|
|Authors:||Srinivasan, K.N. |
|Keywords:||Buthus martensi Karsch|
|Source:||Srinivasan, K.N.,Nirthanan, S.,Gopalakrishnakone, P.,Gwee, M.C.E.,Sasaki, T.,Sato, K.,Cheng, B.,Kini, R.M. (2001). Functional site of bukatoxin, an α-type sodium channel neurotoxin from the Chinese scorpion (Buthus martensi Karsch) venom: Probable role of the52PDKVP56loop. FEBS Letters 494 (3) : 145-149. ScholarBank@NUS Repository. https://doi.org/10.1016/S0014-5793(01)02342-0|
|Abstract:||α-Toxins from scorpion venoms prolong the action potential of excitable cells by blocking sodium channel inactivation. We have purified bukatoxin, an α-toxin from scorpion (Buthus martensi Karsch) venom, to homogeneity. Bukatoxin produced marked relaxant responses in the carbachol-precontracted rat anococcygeus muscle (ACM), which were mediated through the L-arginine-nitric oxide synthase-nitric oxide pathway, consequent to a neuronal release of nitric oxide. Based on the presence of proline residues in the flanking segments of protein-protein interaction sites, we predicted the site between 52PP56 to be the potential interaction site of bukatoxin. A homology model of bukatoxin indicated the presence of this site on the surface. Buka11, a synthetic peptide designed based on this predicted site, produced a concentration-dependent nitric oxide-mediated relaxant response in ACM. Using alanine-substituted peptides, we have shown the importance 53DKV55 flanked by proline residues in the functional site of bukatoxin. © 2001 Federation of European Biochemical Societies.|
|Source Title:||FEBS Letters|
|Appears in Collections:||Staff Publications|
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