TAILIEUCHUNG - Báo cáo khoa học: Solution structure of crotamine, a Na+ channel affecting toxin from Crotalus durissus terrificus venom

Crotamine is a component of the venom of the snakeCro-talus durissus terrificusand it belongs to the myotoxin pro-tein family. It is a 42 amino acid toxin cross-linked by three disulfide bridges and characterized by a mild toxicity (LD50¼820lg per 25 g body weight, . injection) when compared to other members of the same family. Nonethe-less, it possesses a wide spectrum of biological functions. | Eur. J. Biochem. 270 1969-1979 2003 FEBS 2003 doi Solution structure of crotamine a Na channel affecting toxin from Crotalus durissus terrificus venom Giuseppe Nicastro1 2 Lorella Franzoni1 Cesira de Chiara1 Adriana C. Mancin3 Jose R. Giglio3 and Alberto Spisni1 1 Department of Experimental Medicine Section of Chemistry and Structural Biochemistry University of Parma Italy 2Centro Interfacolta Misure University of Parma Italy 3Department of Biochemistry and Immunology University of Sao Paulo Brazil Crotamine is a component of the venom of the snake Cro-talus durissus terrificus and it belongs to the myotoxin protein family. It is a 42 amino acid toxin cross-linked by three disulfide bridges and characterized by a mild toxicity LD50 820 Ig per 25 g body weight . injection when compared to other members of the same family. Nonetheless it possesses a wide spectrum of biological functions. In fact besides being able to specifically modify voltage-sensitive Na channel it has been suggested to exhibit analgesic activity and to be myonecrotic. Here we report its solution structure determined by proton NMR spectroscopy. The secondary structure comprises a short N-terminal a-helix and a small antiparallel triple-stranded b-sheet arranged in an ab1 b2b3 topology never found among toxins active on ion channels. Interestingly some scorpion toxins characterized by a biological activity on Na channels similar to the one reported for crotamine exhibit an a b fold though with a b1ab2b3 topology. In addition as the antibacterial b-defensins crotamine interacts with lipid membranes. A comparison of crotamine with human b-defensins shows a similar fold and a comparable net positive potential surface. To the best of our knowledge this is the first report on the structure of a toxin from snake venom active on Na channel. Keywords b-defensin myotoxin NMR scorpion toxin structure. Despite the fact that Na channels are affected by a large variety of .

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