Solution structure of omega-conotoxin MVIIA using 2D NMR spectroscopy.
The solution structure of omega-conotoxin MVIIA (SNX-111), a peptide toxin from the fish hunting cone snail Conus magus and a high-affinity blocker of N-type calcium channels, was determined by 2D NMR spectroscopy. The backbones of the best 44 structures match with an average pairwise RMSD of 0.59 angstroms. The structures contain a short segment of triple-stranded beta-sheet involving residues 6-8, 20-21, and 24-25. The structure of this toxin is very similar to that of omega-conotoxin GVIA with which is has only 40% sequence homology, but very similar calcium channel binding affinity and selectivity.
Basus
V J
VJ
Department of Pharmaceutical Chemistry, University of California, San Francisco 94143, USA.
Nadasdi
L
L
Ramachandran
J
J
Miljanich
G P
GP
D000595:Amino Acid Sequence; D000818:Animals; D002121:Calcium Channel Blockers / Q000378:metabolism; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D006859:Hydrogen / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D012908:Snails / Q000737:chemistry; D012984:Software; D020866:omega-Conotoxin GVIA; D020960:omega-Conotoxins
D002121:Calcium Channel Blockers; D010455:Peptides; D020960:omega-Conotoxins; C053423:Conus magus toxin; D006859:Hydrogen; D020866:omega-Conotoxin GVIA