TY - JOUR
T1 - Molecular dissection of cholinergic binding sites
T2 - How do snakes escape the effect of their own toxins?
AU - Ohana, Bella
AU - Fraenkel, Yigal
AU - Navon, Gil
AU - Gershoni, Jonathan M.
PY - 1991/8/30
Y1 - 1991/8/30
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0025995917&partnerID=8YFLogxK
U2 - 10.1016/0006-291X(91)91421-8
DO - 10.1016/0006-291X(91)91421-8
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AN - SCOPUS:0025995917
SN - 0006-291X
VL - 179
SP - 648
EP - 654
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 1
ER -