Solution spatial structure of 'long' neurotoxin M9 from the scorpion Buthus eupeus by 1H-NMR spectroscopy.
1H-NMR spectra of Buthus eupeus neurotoxin M9 (66 amino acid residues, four disulfide bonds) reveal two slowly exchangeable conformations at acidic pH. The spatial structure of the conformer prevailing under physiologically relevant conditions has been determined from two-dimensional 1H-NMR data treated by means of a distance geometry algorithm and refined by molecular modelling. Interrelation between the structure and function of mammalian neurotoxin M9 is discussed by comparing its conformation with those of the scorpion insectotoxins which exhibit different biological specificity (insectotoxins v-2, v-3 and I5A).
Pashkov
V S
VS
Shemyakin Institute of Bioorganic Chemistry, U.S.S.R.
Maiorov
V N
VN
Bystrov
V F
VF
Hoang
A N
AN
Volkova
T M
TM
Grishin
E V
EV
D000595:Amino Acid Sequence; D006859:Hydrogen; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008958:Models, Molecular; D011487:Protein Conformation; D012604:Scorpion Venoms; D013329:Structure-Activity Relationship
D012604:Scorpion Venoms; C058936:neurotoxin M9, scorpion; D006859:Hydrogen