Toxin III of the scorpionAndroctonus australis Hector: Proton nuclear magnetic resonance assignments and secondary structure |
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Authors: | Afaf Mikou Steven R LaPlante Eric Guittet Jean-Yves Lallemand Marie-France Martin-Eau Claire Hervé Rochat |
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Institution: | (1) Laboratoire de R.M.N. ICSN CNRS, 1 Av. de la terrasse, F-91190 Gif-sur-Yvette, France;(2) Laboratoire de Biochimie - URA 1455 CNRS, Université d'Aix-Marseille II, Faculté de Médecine Secteur Nord, Bd Pierre Darmard, F-13326 Marseille Cedex 15, France;(3) Present address: Bio-Méga Inc., 2 100 rue Cunard, H7S 2G5 Laval, Québec, Canada |
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Abstract: | Summary
1H NMR has been applied to a3.5 mM, pH 5.4, solution of toxin III (64 amino acids) from venom of the scorpionAndroctonus australis Hector. The resonance assignment strategy began by applying a generalized main-chain directed method for rapid identification and resonance assignments of secondary structures. The remaining resonances were assigned by the sequential method. Major structural features include a helix of 2 1/2 turns (residues 20–28) which is linked by two disulfide bridges to the central strand of a triple-stranded antiparallel -sheet. Turns were identified at residues 15–17, 47–49 and also at residues 51–53. Numerous NOEs have been observed between hydrophobic residues which suggest the presence of a hydrophobic core; these include Leu37, Leu23, Val47, Tyr14, Trp45 and Tyr5. The Trp45 and Tyr5 rings lie orthogonal to one another. No crystal structure has been solved for this AaH III toxin. Comparisons are made with other members of the scorpion toxin family.Thenomenclature used is similar to that described by Wütrich, 1986. |
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Keywords: | Scorpion Toxin NMR Assignment Structure Protein |
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