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Complete amino acid sequence of a new type of lethal neurotoxin from the venom of the funnel‐web spider Atrax robustus
Author(s) -
Sheumack D.D.,
Claassens R.,
Whiteley N.M.,
Howden M.H.H.
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)81132-7
Subject(s) - venom , neurotoxin , spider toxin , cysteine , peptide , spider , chemistry , amino acid , residue (chemistry) , amino acid residue , peptide sequence , biochemistry , stereochemistry , biology , zoology , enzyme , glutamate receptor , receptor , gene
Robustoxin, the lethal neurotoxin isolated from the venom of the male Sydney funnel–web spider, Atrax robustus , is of unique structural type and physiological mode of action. The primary structure of this 42–residue peptide was determined to be H 2 N–Cys–Ala–Lys–Lys–Arg–Asn–Trp–Cys–Gly–Lys 10 –Asn–Glu–Asp–Cys–Cys–Cys–Pro–Met–Lys–Cys 20 –Ile–Tyr–Ala–Trp–Tyr–Ala–Trp–Tyr–Asn–Gln–Gln–Gly–Ser 30 –Cys–Gln–Thr–Thr–Ile–Thr–Gly–Leu–Phe–Lys 40 –Lys–Lys–Cys–H The disposition of disulphide–bridged cysteine residues at both the amino– and carboxy–termini and as a triplet at residues 14–16 appears to have no precedent amongst neurotoxins.