2e2s: Difference between revisions

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==Overview==

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.

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.

==About this Structure==

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[[Category: toxin]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-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.
+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.
 ==About this Structure==
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 [[Category: toxin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:06:02 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:05:22 2008''