| Title : Molecular dissection of cholinergic binding sites: how do snakes escape the effect of their own toxins? - Ohana_1991_Biochem.Biophys.Res.Commun_179_648 |
| Author(s) : Ohana B , Fraenkel Y , Navon G , Gershoni JM |
| Ref : Biochemical & Biophysical Research Communications , 179 :648 , 1991 |
|
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. |
| PubMedSearch : Ohana_1991_Biochem.Biophys.Res.Commun_179_648 |
| PubMedID: 1883386 |
Ohana B, Fraenkel Y, Navon G, Gershoni JM (1991)
Molecular dissection of cholinergic binding sites: how do snakes escape the effect of their own toxins?
Biochemical & Biophysical Research Communications
179 :648
Ohana B, Fraenkel Y, Navon G, Gershoni JM (1991)
Biochemical & Biophysical Research Communications
179 :648