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Solution structure of agelenin, an insecticidal peptide isolated from the spider Agelena opulenta , and its structural similarities to insect‐specific calcium channel inhibitors
Author(s) -
Yamaji Nahoko,
Sugase Kenji,
Nakajima Terumi,
Miki Takafumi,
Wakamori Minoru,
Mori Yasuo,
Iwashita Takashi
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.06.077
Subject(s) - pharmacophore , spider , antiparallel (mathematics) , peptide , calcium channel , stereochemistry , chemistry , spider toxin , venom , insect , disulfide bond , biophysics , calcium , biochemistry , biology , physics , zoology , ecology , receptor , organic chemistry , quantum mechanics , magnetic field , glutamate receptor
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.