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Science 6 December 1991:
Vol. 254. no. 5037, pp. 1521 - 1523
DOI: 10.1126/science.1720574
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Articles

Science, Vol 254, Issue 5037, 1521-1523
Copyright © 1991 by American Association for the Advancement of Science

articles

Refined structure of charybdotoxin: common motifs in scorpion toxins and insect defensins

F Bontems, C Roumestand, B Gilquin, A Menez, and F Toma

Departement d'Ingenierie et d'Etudes des Proteines, Gif sur Yvette, France.

Conflicting three-dimensional structures of charybdotoxin (Chtx), a blocker of K+ channels, have been previously reported. A high-resolution model depicting the tertiary structure of Chtx has been obtained by DIANA and X-PLOR calculations from new proton nuclear magnetic resonance (NMR) data. The protein possesses a small triple-stranded antiparallel beta sheet linked to a short helix by two disulfides and to an extended fragment by one disulfide, respectively. This motif also exists in all known structures of scorpion toxins, irrespective of their size, sequence, and function. Strikingly, antibacterial insect defensins also adopt this folding pattern.


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   Abstract »    Full Text »    PDF »


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Science. ISSN 0036-8075 (print), 1095-9203 (online)