1AXH

ATRACOTOXIN-HVI FROM HADRONYCHE VERSUTA (AUSTRALIAN FUNNEL-WEB SPIDER, NMR, 20 STRUCTURES

Summary for 1AXH

• Entry DOI: 10.2210/pdb1axh/pdb
• NMR Information: BMRB: 5702,6192,6194
• Descriptor: ATRACOTOXIN-HVI (1 entity in total)
• Functional Keywords: neurotoxin, insecticidal toxin, cystine knot, funnel-web
• Biological source: Hadronyche versuta
• Total number of polymer chains: 1
• Total formula weight: 4058.45

Authors

Fletcher, J.I.,O'Donoghue, S.I.,Nilges, M.,King, G.F. (deposition date: 1996-11-04, release date: 1997-11-12, Last modification date: 2024-10-30)

Primary citation

Fletcher, J.I.,Smith, R.,O'Donoghue, S.I.,Nilges, M.,Connor, M.,Howden, M.E.,Christie, M.J.,King, G.F.
The structure of a novel insecticidal neurotoxin, omega-atracotoxin-HV1, from the venom of an Australian funnel web spider.
Nat.Struct.Biol., 4:559-566, 1997

PubMed Abstract: A family of potent insecticidal toxins has recently been isolated from the venom of Australian funnel web spiders. Among these is the 37-residue peptide omega-atracotoxin-HV1 (omega-ACTX-HV1) from Hadronyche versuta. We have chemically synthesized and folded omega-ACTX-HV1, shown that it is neurotoxic, ascertained its disulphide bonding pattern, and determined its three-dimensional solution structure using NMR spectroscopy. The structure consists of a solvent-accessible beta-hairpin protruding from a disulphide-bonded globular core comprising four beta-turns. The three intramolecular disulphide bonds from a cystine knot motif similar to that seen in several other neurotoxic peptides. Despite limited sequence identity, omega-ACTX-HV1 displays significant structural homology with the omega-agatoxins and omega-conotoxins, both of which are vertebrate calcium channel antagonists; however, in contrast with these toxins, we show that omega-ACTX-HV1 inhibits insect, but not mammalian, voltage-gated calcium channel currents.

PubMed: 9228949
DOI: 10.1038/nsb0797-559

Experimental method

SOLUTION NMR