Solution structure of omega-conotoxin MVIIC determined by NMR.
The solution structure of the P- and Q-type Ca2+ channel blocker, omega-conotoxin MVIIC (a peptidic neurotoxin composed of 26 amino acid residues), has been determined by 1H-NMR and simulated annealing calculations. The resulting calculated structures converged very well to a conformation with an average value of pairwised RMSD for N, C alpha and C' of 0.62 A. Lys-25 is buried in the molecule and less flexible so that among the four Lys residues, its side chain provides the lowest reactivity on biotinylation and the mono-biotinylation in this residue less influences the biological activity.
Nemoto
N
N
Institute for Protein Research, Osaka University, Japan.
Kubo
S
S
Yoshida
T
T
Chino
N
N
Kimura
T
T
Sakakibara
S
S
Kyogoku
Y
Y
Kobayashi
Y
Y
D000595:Amino Acid Sequence; D002121:Calcium Channel Blockers / Q000737:chemistry; D003198:Computer Simulation; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008958:Models, Molecular; D008969:Molecular Sequence Data; D008978:Mollusk Venoms / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D012996:Solutions; D020960:omega-Conotoxins
D002121:Calcium Channel Blockers; D008978:Mollusk Venoms; D010455:Peptides; D012996:Solutions; D020960:omega-Conotoxins; C075851:omega-conotoxin-MVIIC