Three-Dimensional Structure of ω-Conotoxin GVIA Determined by 1H-NMR

摘要: omega-Conotoxin GVIA, a peptide of 27 amino acid residues and three disulfide bridges, has been studied by NMR techniques. The complete assignment the corresponding proton spectra was performed two-dimensional sequence specific methods at 288 K pH 3.5. On basis 169 distance restraints derived from this analysis, three-dimensional structure obtained. A total 30 initial structures were generated geometry further refined restrained energy minimization techniques yielding final set 8 structures. mean root-mean-square deviation between each atomic coordinates for all is 0.82 +/- 0.06 backbone atoms 1.45 0.18 non-H atoms. shows globular folding pattern that stabilized linkages number intramolecular hydrogen bonds. 14 hydroxyl groups are found periphery fully exposed to solvent. These groups, together with charged side chains Lys Arg emerging radially core, provide recognition elements interaction toxin neuronal calcium channels.