2e2s: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
New page: left|200px<br /><applet load="2e2s" size="350" color="white" frame="true" align="right" spinBox="true" caption="2e2s" /> '''Solution structure of agelenin, an insectici...
 
No edit summary
Line 4: Line 4:


==Overview==
==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==
==About this Structure==
Line 18: Line 18:
[[Category: toxin]]
[[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''

Revision as of 18:05, 21 February 2008

File:2e2s.jpg


2e2s

Drag the structure with the mouse to rotate

Solution structure of agelenin, an insecticidal peptide from the venom of Agelena opulenta

OverviewOverview

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 StructureAbout this Structure

2E2S is a Single protein structure of sequence from Agelena opulenta. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Thu Feb 21 17:05:22 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA