2E2S
Solution structure of agelenin, an insecticidal peptide from the venom of Agelena opulenta
Summary for 2E2S
| Entry DOI | 10.2210/pdb2e2s/pdb |
| Descriptor | Agelenin (1 entity in total) |
| Functional Keywords | cystine knot, presynaptic calcium channel inhibitor, toxin |
| Biological source | Allagelena opulenta |
| Cellular location | Secreted: P31328 |
| Total number of polymer chains | 1 |
| Total formula weight | 3829.53 |
| Authors | Yamaji, N. (deposition date: 2006-11-17, release date: 2007-08-07, Last modification date: 2024-10-30) |
| Primary citation | Yamaji, N.,Sugase, K.,Nakajima, T.,Miki, T.,Wakamori, M.,Mori, Y.,Iwashita, T. Solution structure of agelenin, an insecticidal peptide isolated from the spider Agelena opulenta, and its structural similarities to insect-specific calcium channel inhibitors Febs Lett., 581:3789-3794, 2007 Cited by PubMed 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. PubMed: 17644092DOI: 10.1016/j.febslet.2007.06.077 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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