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Discovery and characterization of a family of insecticidal neurotoxins with a rare vicinal disulfide bridge
- Source :
- Nature Structural Biology. 7:505-513
- Publication Year :
- 2000
- Publisher :
- Springer Science and Business Media LLC, 2000.
-
Abstract
- We have isolated a family of insect-selective neurotoxins from the venom of the Australian funnel-web spider that appear to be good candidates for biopesticide engineering. These peptides, which we have named the Janus-faced atracotoxins (J-ACTXs), each contain 36 or 37 residues, with four disulfide bridges, and they show no homology to any sequences in the protein/DNA databases. The three-dimensional structure of one of these toxins reveals an extremely rare vicinal disulfide bridge that we demonstrate to be critical for insecticidal activity. We propose that J-ACTX comprises an ancestral protein fold that we refer to as the disulfide-directed beta-hairpin.
- Subjects :
- Models, Molecular
Insecticides
Protein Folding
Insecta
Amino Acid Motifs
Molecular Sequence Data
Neurotoxins
Beta sheet
Spider Venoms
Venom
Biochemistry
Protein Structure, Secondary
Homology (biology)
Evolution, Molecular
Lethal Dose 50
Mice
chemistry.chemical_compound
Species Specificity
Structural Biology
Genetics
Animals
Receptors, Cholinergic
Amino Acid Sequence
Disulfides
Binding site
Nuclear Magnetic Resonance, Biomolecular
Chromatography, High Pressure Liquid
Neurons
Binding Sites
Chemistry
Cystine knot
Protein Structure, Tertiary
Inhibitor cystine knot
Sequence Alignment
Vicinal
DNA
Subjects
Details
- ISSN :
- 10728368
- Volume :
- 7
- Database :
- OpenAIRE
- Journal :
- Nature Structural Biology
- Accession number :
- edsair.doi.dedup.....2ec2a8d5822c6d52b33d2dad944be395