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Solution structure of BTK-2, a novel hK(v)1.1 inhibiting scorpion toxin, from the eastern Indian scorpion Mesobuthus tamulus

Kumar, Senthil G and Upadhyay, Sanjeev and Mathew, MK and Sarma, Siddhartha P (2011) Solution structure of BTK-2, a novel hK(v)1.1 inhibiting scorpion toxin, from the eastern Indian scorpion Mesobuthus tamulus. In: Biochimica et Biophysica Acta (BBA) - Proteins & Proteomics, 1814 (4). pp. 459-469.

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Official URL: http://dx.doi.org/10.1016/j.bbapap.2011.01.006


The three dimensional structure of a 32 residue three disulfide scorpion toxin, BTK-2, from the Indian red scorpion Mesobuthus tamulus has been determined using isotope edited solution NMR methods. Samples for structural and electrophysiological studies were prepared using recombinant DNA methods. Electrophysiological studies show that the peptide is active against hK(v)1.1 channels. The structure of BTK-2 was determined using 373 distance restraints from NOE data, 66 dihedral angle restraints from NOE, chemical shift and scalar coupling data, 6 constraints based on disulfide linkages and 8 constraints based on hydrogen bonds. The root mean square deviation (r.m.s.d) about the averaged co-ordinates of the backbone (N, C-alpha, C') and all heavy atoms are 0.81 +/- 0.23 angstrom and 1.51 +/- 0.29 angstrom respectively. The backbone dihedral angles (phi and psi) for all residues occupy the favorable and allowed regions of the Ramachandran map. The three dimensional structure of BTK-2 is composed of three well defined secondary structural regions that constitute the alpha-beta-beta, structural motif. Comparisons between the structure of BTK-2 and other closely related scorpion toxins pointed towards distinct differences in surface properties that provide insights into the structure-function relationships among this important class of voltage-gated potassium channel inhibiting peptides. (C) 2011 Elsevier B.V. All rights reserved.

Item Type: Journal Article
Publication: Biochimica et Biophysica Acta (BBA) - Proteins & Proteomics
Publisher: Elsevier Science B.V.
Additional Information: Copyright of this article belongs to Elsevier Science B.V.
Keywords: NMR spectroscopy;Isotopically enriched peptide;Disulfide rich toxin;Solution structure;Folding of disulfide rich peptide
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited: 20 Apr 2011 05:18
Last Modified: 20 Apr 2011 05:18
URI: http://eprints.iisc.ac.in/id/eprint/36974

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