Molecular dissection of cholinergic binding sites: How do snakes escape the effect of their own toxins?

Bella Ohana, Yigal Fraenkel, Gil Navon, Jonathan M. Gershoni

Research output: Contribution to journalArticlepeer-review

Abstract

Snakes have evolved a novel binding site demonstrating selective biorecognition. The snake nicotinic acetylcholine receptor is sensitive to acetylcholine while resistant to the effect of the lethal neurotoxins secreted in their own venom. By subjecting recombinant binding sites to point mutagenesis, biochemical analyses and NMR spectroscopy the binding characteristics of three cholinergic ligands have been measured. The amino acid residue at position 189 has been found to be of particular importance to toxin binding.

Original languageEnglish
Pages (from-to)648-654
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume179
Issue number1
DOIs
StatePublished - 30 Aug 1991

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