AI Article Synopsis
- Huwentoxin-XI, a toxin from the Chinese bird spider, has antiprotease and potassium channel blocking activities.
- The solution structure of huwentoxin-XI was determined using NMR after expressing it in yeast, employing a 15N labeling strategy for resonance assignments.
- The secondary structure analysis revealed an N-terminal 310-helix, a C-terminal alpha-helix, and a triple-stranded antiparallel beta-sheet, providing key insights for its final structural determination.
Article Abstract
Huwentoxin-XI purified from the Chinese bird spider Ornithoctonus huwena is a toxin with both antiprotease activity and potassium channel blocking activity. To determine its solution structure, huwentoxin-XI was expressed in a yeast eukaryotic expression system and studied by NMR. The 15N labeling strategy was used to facilitate the process of resonance assignments. The nearly complete sequence-specific assignments of proton and nitrogen resonances were obtained by analyzing a series of two-dimensional (2D) and three-dimensional (3D) spectra, including DQF-COSY, TOCSY, NOESY, 15N-1H HSQC, 15N-1H HNHA, 15N-1H HNHB, 15N-1H TOCSY-HSQC and 15N-1H NOESY-HSQC spectra. Secondary structure analysis of huwentoxin-XI showed that it mainly contains an N-terminal 310-helix from Thr3 to Arg5 and a C-terminal alpha-helix from Gln45 to Cys52, plus a triple-stranded antiparallel beta-sheet of Glu18-Asn23, Thr26-Ile31 and Asn40-Lys41. These studies provide a solid basis for the final structure determination of huwentoxin-XI.
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| http://dx.doi.org/10.1111/j.1745-7270.2006.00191.x | DOI Listing |
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