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The disulfide bridges of toxin 2 from the scorpion Centruroides noxius Hoffmann and its three‐dimensional structure calculated using the coordinates of variant 3 from Centruroides sculpturatus
Author(s) -
Gurrola G.B.,
Moreno-Hagelsieb G.,
Zamudio F.Z.,
García M.,
Soberon X.,
Possani L.D.
Publication year - 1994
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(94)00507-9
Subject(s) - scorpion , scorpion toxin , toxin , chemistry , venom , stereochemistry , cleavage (geology) , peptide sequence , disulfide bond , amino acid , biochemistry , biology , paleontology , fracture (geology) , gene
The disulfide bridges of toxin 2 from the venom of the scorpion Centruroides noxius Hoffmann were found by amino acid sequence determination of fragments of native toxin, produced by enzymatic cleavage and separated by high‐performance liquid chromatography (HPLC). They are: Cys 12 ‐Cys 65 , Cys 16 ‐Cys 41 , Cys 25 ‐Cys 46 and Cys 29 ‐Cys 48 . The coordinates of the X‐ray diffraction structure of toxin variant 3 of C. sculpturatus [(1980) Proc. Natl. Acad. Sci. USA 77, 6496–6500] were used to construct a three dimensional model of toxin 2. All the amino acid replacements were easily accommodated, and the modeled structure reveals a clustered pattern of sequence variation, which may help to identify residues responsible for functional differences among toxins of mammals and insects.