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Protein & Peptide Letters


ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

Sequence-specific 1H-NMR Assignment and Determination of the Secondary Structure of Hainantoxin-III from the Spider Ornithoctonus hainana

Author(s): Zhonghua Liu, Qi Zhu, Weijun Hu and Songping Liang

Volume 20, Issue 7, 2013

Page: [761 - 766] Pages: 6

DOI: 10.2174/0929866511320070005


Hainantoxin-III (HNTX-III) purified from the venom of the spider Ornithoctonus hainana is a novel neurotoxin preferentially inhibiting tetrodotoxin-sensitive voltage-gated sodium channels in rat dorsal root ganglion cells. The structure of this toxin in aqueous solution was investigated using 2-D 1H-NMR techniques. The complete sequencespecific assignments of proton resonances in the 1H-NMR spectra were obtained by analyzing a series of 2-D spectra, including DQF-COSY, TOCSY and NOESY spectra, in H2O or D2O. All the backbone protons and more than 95% of the side-chain protons have been assigned by dαN, dβN, and dNN connectivities in NOESY spectrum. Furthermore, the secondary structure of HNTX-III was identified from NMR data. It consists mainly of a short triple-stranded antiparallel β-sheet formed by Asp7 to Cys9, Tyr21 to Ser23, and Lys27 to Val30. Because HNTX-III shares high sequence identity (>70%) with HWTX-I and HNTX-I, we proposed that they all share a structural scaffold known as the inhibitor cystine knot architectural motif. This study provides a basis for the further determination of the solution conformation of HNTX-III.

Keywords: 2-D nuclear magnetic resonance (NMR), hainantoxin-III (HNTX-III), sequence-specific assignment, secondary structure.

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