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Crystal Structure of a Recombinant alpha-insect Toxin BmKaIT1 from the scorpion Buthus martensii Karsch
Structural highlights
FunctionSC12_MESMA Alpha toxins bind voltage-independently at site-3 of sodium channels (Nav) and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission (By similarity). Shows a high toxicity toward insects and moderate toxicity against mammals.[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 PubMedAlpha-insect scorpion toxins are a distinct group of scorpion neurotoxins for which no crystal structures are yet available. A novel alpha-insect toxin named BmKalphaIT1 from the scorpion Buthus martensii Karsch (BmK) has been expressed as an inclusion body in Escherichia coli and purified by chromatography after renaturation. Recombinant BmKalphaIT1 (rBmKaIT1) was crystallized using the vapour-diffusion technique in hanging drops at 296 K. The crystals, which were grown in sodium phosphate, belonged to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 30.24 (1), b = 36.51 (3), c = 57.08 (2) A. Diffraction data were collected to 2.1 A resolution using synchrotron radiation. There appears to be one rBmKalphaIT1 molecule in the asymmetric unit. Crystallization and preliminary crystallographic study of rBmKalphaIT1, a recombinant alpha-insect toxin from the scorpion Buthus martensii Karsch.,Huang Y, Huang Q, Chen H, Tang Y, Miyake H, Kusunoki M Acta Crystallogr D Biol Crystallogr. 2003 Sep;59(Pt 9):1635-6. Epub 2003, Aug 19. PMID:12925796[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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