Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2050633 | FEBS Letters | 2007 | 6 Pages |
Abstract
Agelenin, isolated from the Agelenidae spider Agelena opulenta, is a peptide composed of 35 amino acids. We determined the three-dimensional structure of agelenin using two-dimensional NMR spectroscopy. The structure is composed of a short antiparallel β-sheet and four β-turns, which are stabilized by three disulfide bonds. Agelenin has characteristic residues, Phe9, Ser28 and Arg33, which are arranged similarly to the pharmacophore of the insect channel inhibitor, ω-atracotoxin-Hv1a. These observations suggest that agelenin and ω-atracotoxin-Hv1a bind to insect calcium channels in a similar manner. We also suggest that another mode of action may operate in the channel inhibition by ω-agatoxin-IVA and ω-atracotoxin-Hv2a.
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Authors
Nahoko Yamaji, Kenji Sugase, Terumi Nakajima, Takafumi Miki, Minoru Wakamori, Yasuo Mori, Takashi Iwashita,