Premium
Constant and hypervariable regions in conotoxin propeptides.
Author(s) -
Woodward S.R.,
Cruz L.J.,
Olivera B.M.,
Hillyard D.R.
Publication year - 1990
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1990.tb08204.x
Subject(s) - salt lake , library science , sociology , geology , computer science , paleontology , structural basin
Conotoxins are small cysteine rich peptides found in the venom of the predatory cone snails (Conus) which have prove to be useful high affinity ligands for various receptors and ion channels. The first cloning data for conotoxins, reported here, were obtained for the King‐Kong peptide, a 27 amino acid conotoxin found in the venom of the cloth‐of‐gold cone, Conus textile. Analysis of cDNA clones of the King‐Kong peptide revealed a family of related toxin transcripts. Three different propeptide cDNA sequences were obtained; only one of these encoded sequence for the King‐Kong peptide. The other cDNA sequences encoded two different peptides (KK‐1 and KK‐2). When the predicted propeptide sequences are compared, well defined conserved and hypervariable regions can be identified. The hypervariable regions comprise four regions between Cys residues in the final peptide toxins; the remainder of the propeptide sequences, i.e. the excised N‐terminal regions and the disulfide bonded Cys residues, are highly conserved. We suggest that the conserved regions may direct the formation of a specific disulfide configuration in the King‐Kong family of conotoxins.