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• W2073609664 abstract "The nicotinic acetylcholine receptors (nAChRs) and glutamate receptors are ligand-gated cation channels composed of five separate polypeptide chains. A 43 kDa protein of unknown function is noncovalently associated with the cytoplasmic side of nAChR in vivo. The venoms of many wasps and spiders contain toxins that block the activity of these channels. Philanthotoxin-433 (PhTX-433) is a non-competitive channel blocker found in the venom of the wasp Philanthus. We have used a photolabile derivative to investigate how PhTX-433 interacts with nAChRs.A radiolabeled PhTX analog, containing a photolabile group substituted on one of its aromatic rings, photocrosslinked to all five subunits (alpha, alpha 1, beta, gamma, delta) of purified nAChR in the absence of the 43 kDa protein. In the presence of the 43 kDa protein, the alpha subunit was preferentially labeled. Proteolysis of the receptor after crosslinking indicated that the hydrophobic end (head) of the PhTx-433 analog bound to the cytoplasmic loop(s) of the alpha-subunit. Binding is inhibited by other non-competitive channel blockers such as the related polyamine-amide toxins from spiders and chlorpromazine.These results, coupled with previous structure/activity studies, lead to a putative model of the binding of PhTx and related polyamine toxins to nAChRs in vitro. The 43 kDa protein appears to influence the orientation of toxin binding. Further binding studies are necessary to confirm the model and to define how toxins enter the receptor and how they are oriented within it. A precise understanding of ligand/receptor interaction is crucial for the design of drugs specific for a particular subtype of receptor." @default.
• W2073609664 created "2016-06-24" @default.
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• W2073609664 date "1995-01-01" @default.
• W2073609664 modified "2023-09-26" @default.
• W2073609664 title "Labeling studies of photolabile philanthotoxins with nicotinic acetylcholine receptors: mode of interaction between toxin and receptor" @default.
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• W2073609664 doi "https://doi.org/10.1016/1074-5521(95)90077-2" @default.
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