Sandbox 174: Difference between revisions
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Elapidae neurotoxins bind specifically and tightly (with a very high affinity) in a non-covalent manner to the nicotinic acetylcholine receptors in cholinergic synapses of their victims. This prevents normal neurotransmitter-induced channel opening, which in turn blocks postsynaptic membrane depolarization<ref name="main">Love, A.R. and Stroud, R.M. (1986) The Crystal Structure of α-Bungarotoxin at 2.5 Å resolution: Relation to Solution Structure and Binding to Acetylcholine Receptor. ''Protein Eng'' '''1''', 37-46.</ref>, classifying the molecule as a postsynaptic neurotoxin. | Elapidae neurotoxins bind specifically and tightly (with a very high affinity) in a non-covalent manner to the nicotinic acetylcholine receptors in cholinergic synapses of their victims. This prevents normal neurotransmitter-induced channel opening, which in turn blocks postsynaptic membrane depolarization<ref name="main">Love, A.R. and Stroud, R.M. (1986) The Crystal Structure of α-Bungarotoxin at 2.5 Å resolution: Relation to Solution Structure and Binding to Acetylcholine Receptor. ''Protein Eng'' '''1''', 37-46.</ref>, classifying the molecule as a postsynaptic neurotoxin. | ||
==neuromuscular acetylcholine receptor binding== | ==neuromuscular acetylcholine receptor binding== | ||
The irriversable and competitive binding to the acetylcholine receptor by α-BTG can be devastating to an organisms health due to its ability to block the receptors activity. | |||
http://www.ncbi.nlm.nih.gov/pubmed/12885641 | |||
==α7 nicotinic acetylcholine receptor binding== | ==α7 nicotinic acetylcholine receptor binding== | ||
