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A proposal for the structure of conotoxin ‐ a potent antagonist of the nicotinic acetylcholine receptor
Author(s) -
Hider R.C.
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)80602-5
Subject(s) - conotoxin , nicotinic acetylcholine receptor , venom , circular dichroism , chemistry , postsynaptic potential , antagonist , cystine , acetylcholine receptor , nicotinic agonist , biochemistry , stereochemistry , biophysics , receptor , pharmacology , biology , cysteine , enzyme
Conotoxin, a thirteen residue neurotoxic peptide, is demonstrated, by circular dichroism measurements, to possess a high content of α‐hélix. The location of this helix in the sequence is severely limited by the structural preferences of individual amino acids and by the positioning of the two cystine links. Comparisons are made between the reactive site of elapidae snake venom postsynaptic neurotoxins and the surface of the conotoxin molecule.