Solution Structure of the Noncompetitive Skeletal Muscle Nicotinic Acetylcholine Receptor Antagonist Psi-conotoxin PIIIE
An Improved Solution Structure for psi-Conotoxin Piiie
Three-dimensional Solution Structure of Conotoxin psi-PIIIE, an Acetylcholine Gated Ion Channel Antagonist
A Noncompetitive Peptide Inhibitor of the Nicotinic Acetylcholine Receptor from Conus purpurascens Venom
1AS5 contains the original structures calculated for psi-conotoxin PIIIE.
Solid phase chemical synthesis was used to incorporate 3-13C-labeled cysteine at positions 4 and 21. The sequence is the same as the native peptide from CONUS PURPURASCENS (PURPLE CONE).
This structure was determined using isotopic filtration and isotope-selected 1H observation in addition to standard homonuclear techniques.
back calculated data agree with experimental NOESY spectrum, structures with the least restraint violations, structures with the lowest energy
These structures are based on 566 NOE-derived distance restraints, 9 restraints on phi derived from J-coupling, and 13 restraints on chi1 determined from J-coupling and NOE volumes.
distance geometry molecular dynamics relaxation matrix distance geometry simulated annealing
16 mM psi-conotoxin PIIIE [4,21] 3-13C-Cys; TFA added to pH 3.5
16 mM psi-conotoxin PIIIE [4,21] 3-13C-Cys
MULTIPLE DISULFIDE BONDS, AMIDATED C-TERMINUS, TOXIN