1H nuclear-magnetic-resonance studies of the three-dimensional structure of the cardiotoxin CTXIIb from Naja mossambica mossambica in aqueous solution and comparison with the crystal structures of homologous toxins.
Using the previously reported sequence-specific 1H-NMR assignments, structural constraints for the cardiotoxin CTXIIb from Naja mossambica mossambica were collected. These include distance constraints from nuclear Overhauser enhancement measurements both in the laboratory and in the rotating frame, dihedral angle constraints derived from spin-spin coupling constants, and constraints from hydrogen bonds and disulfide bridges. Structure calculations with the distance geometry program DISMAN confirmed the presence of the previously identified antiparallel beta-sheets formed by residues 1-5 and 10-14, and by 20-27, 35-39 and 49-55, and established the nature of the connections between the individual beta-strands. These include a right-handed crossover between the two peripheral strands in the triple-stranded beta-sheet, and a type I tight turn immediately preceding the beta-strand 49-55. The spatial arrangement of the polypeptide backbone in the solution structure of CTXIIb is closely similar to that in the crystal structure of the homologous cardiotoxin VII4 from the same species. In an Appendix the origin of the large pH dependence of two amide proton chemical shifts in CTXIIb is explained.
Steinmetz
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Institut für Molekularbiologie und Biophysik, Eidgenössische Technische Hochschule Zürich-Hönggerberg, Switzerland.
Bougis
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Rochat
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Redwine
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Braun
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Wüthrich
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D000818:Animals; D004179:Cobra Cardiotoxin Proteins / Q000032:analysis*; D004546:Elapid Venoms / Q000032:analysis*; D009682:Magnetic Resonance Spectroscopy; D010455:Peptides / Q000032:analysis; D011487:Protein Conformation; D012996:Solutions
D004179:Cobra Cardiotoxin Proteins; D004546:Elapid Venoms; D010455:Peptides; D012996:Solutions