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• W2019467184 abstract "Alpha-toxins from scorpion venoms prolong the action potential of excitable cells by blocking sodium channel inactivation. We have purified bukatoxin, an alpha-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 (52)PP(56) 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 (53)DKV(55) flanked by proline residues in the functional site of bukatoxin." @default.
• W2019467184 created "2016-06-24" @default.
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• W2019467184 date "2001-04-10" @default.
• W2019467184 modified "2023-09-26" @default.
• W2019467184 title "Functional site of bukatoxin, an α-type sodium channel neurotoxin from the Chinese scorpion (<i>Buthus martensi</i>Karsch) venom: probable role of the⁵²PDKVP⁵⁶loop" @default.
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• W2019467184 doi "https://doi.org/10.1016/s0014-5793(01)02342-0" @default.
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