Work

Solution structure of agelenin, an insecticidal peptide isolated from the spider Agelena opulenta, and its structural similarities to insect‐specific calcium channel inhibitors

Year: 2007

Type: article

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 beta-sheet and four beta-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, omega-atracotoxin-Hv1a. These observations suggest that agelenin and omega-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 omega-agatoxin-IVA and omega-atracotoxin-Hv2a.

Source: FEBS Letters

DOI: 10.1016/j.febslet.2007.06.077

Authors: Nahoko Yamaji, Kenji Sugase, Terumi Nakajima, Takafumi Miki, Minoru Wakamori, Yasuo Mori, Takashi Iwashita

Institution: Kyoto University

Language: English

Topic: Venomous Animal Envenomation and Studies

Subfield: Toxicology

Field: Pharmacology, Toxicology and Pharmaceutics

Domain: Life Sciences

Open Access status: bronze

OpenAlex ID: W2075609786

FWCI: 1.264

Cites: 28

Cited by: 10

Related to: 10