Solution conformation of leiurotoxin I (scyllatoxin) by 1H nuclear magnetic resonance. Resonance assignment and secondary structure.
A proton NMR study at 500 MHz of leiurotoxin I in water is presented. Nearly complete sequence-specific assignments of the individual backbone and side-chain proton resonances were achieved using through-bond and through-space connectivities obtained from standard two-dimensional NMR techniques. The secondary structure of this toxin is inferred from a combination of short-range nuclear Overhauser enhancements, scalar couplings and proton/deuteron exchange rates. Three disulfide bridges locate the N-terminal part (that is alpha-helical from residue 6 to 16) on one side of a C-terminal two stranded antiparallel beta sheet (from Leu18 to Val29). The latter features a tight turn at Gly23-Asp24.
Martins
J C
JC
Laboratory of Organic Chemistry, State University Ghent, Belgium.
Zhang
W G
WG
Tartar
A
A
Lazdunski
M
M
Borremans
F A
FA
D001030:Apamin / Q000031:analogs & derivatives / Q000032:analysis; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D015394:Molecular Structure; D011485:Protein Binding; D011487:Protein Conformation; D011522:Protons; D012604:Scorpion Venoms / Q000032:analysis* / Q000633:toxicity; D012996:Solutions; D013052:Spectrometry, X-Ray Emission
D011522:Protons; D012604:Scorpion Venoms; D012996:Solutions; C056574:leiurotoxin I; D001030:Apamin