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Publication Type : Journal Article
Publisher : WILEY-VCH Verlag
Source : Chemistry & Biodiversity, WILEY-VCH Verlag, Volume 2, Number 4, p.535–556 (2005)
Url : http://dx.doi.org/10.1002/cbdv.200590035
Campus : Amritapuri
School : School of Biotechnology
Center : Biotechnology
Department : biotechnology
Year : 2005
Abstract : The three-dimensional (3D) NMR solution structure (MeOH) of the highly hydrophobic δ-conotoxin δ-Am2766 from the molluscivorous snail Conus amadis has been determined. Fifteen converged structures were obtained on the basis of 262 distance constraints, 25 torsion-angle constraints, and ten constraints based on disulfide linkages and H-bonds. The root-mean-square deviations (rmsd) about the averaged coordinates of the backbone (N, Cα, C) and (all) heavy atoms were 0.62±0.20 and 1.12±0.23 Å, respectively. The structures determined are of good stereochemical quality, as evidenced by the high percentage (100%) of backbone dihedral angles that occupy favorable and additionally allowed regions of the Ramachandran map. The structure of δ-Am2766 consists of a triple-stranded antiparallel β-sheet, and of four turns. The three disulfides form the classical ‘inhibitory cysteine knot’ motif. So far, only one tertiary structure of a δ-conotoxin has been reported; thus, the tertiary structure of δ-Am2766 is the second such example.Another Conus peptide, Am2735 from C. amadis, has also been purified and sequenced. Am2735 shares 96% sequence identity with δ-Am2766. Unlike δ-Am2766, Am2735 does not inhibit the fast inactivation of Na+ currents in rat brain Nav1.2 Na+ channels at concentrations up to 200 nM.
Cite this Research Publication : S. P. Sarma, G. Kumar, S., Sudarslal, S., Iengar, Prathima, Ramasamy, P., Sikdar, S. K., Krishnan, K. S., and Balaram, P., “Solution Structure of δ-Am2766: A Highly Hydrophobic δ-Conotoxin from Conus amadis That Inhibits Inactivation of Neuronal Voltage-Gated Sodium Channels”, Chemistry & Biodiversity, vol. 2, pp. 535–556, 2005