2e2s
From Proteopedia
Solution structure of agelenin, an insecticidal peptide from the venom of Agelena opulenta
Structural highlights
Function[TXAG_ALLOP] Insect-selective toxin causing rapid but reversible paralysis in crickets. Suppresses the excitatory postsynaptic potentials evoked in lobster neuromuscular synaptic preparations, possibly by blocking the presynaptic calcium channel (Cav). Induces instantaneous reversible paralysis when injected into crickets.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedAgelenin, 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. Solution structure of agelenin, an insecticidal peptide isolated from the spider Agelena opulenta, and its structural similarities to insect-specific calcium channel inhibitors.,Yamaji N, Sugase K, Nakajima T, Miki T, Wakamori M, Mori Y, Iwashita T FEBS Lett. 2007 Aug 7;581(20):3789-94. Epub 2007 Jul 10. PMID:17644092[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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