Agonist-induced changes in the structure of the acetylcholine receptor M2 regions revealed by photoincorporation of an uncharged nicotinic noncompetitive antagonist

To characterize structural changes induced in the nicotinic acetylcholine receptor (AChR) by agonists, we have mapped the sites of photoincorporation of the cholinergic noncompetitive antagonist 3-(trifluoromethyl)-3-(m-[125I]iodophenyl)diazirine (]125I]TID) in the presence and absence of 50 microM...

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Veröffentlicht in:	The Journal of biological chemistry 1992-08, Vol.267 (22), p.15770-15783
Hauptverfasser:	WHITE, B. H, COHEN, J. B
Format:	Artikel
Sprache:	eng
Schlagworte:	acetylcholine agonists Amino Acid Sequence Animals Azirines - metabolism binding Binding Sites Biological and medical sciences Carbachol - pharmacology Cell Membrane - metabolism Cell receptors Cell structures and functions Cyanogen Bromide Electric Organ - metabolism Fundamental and applied biological sciences. Psychology Iodine Radioisotopes Macromolecular Substances Models, Structural Molecular and cellular biology Molecular Sequence Data Monoamines receptors (catecholamine, serotonine, histamine, acetylcholine) Peptide Fragments - isolation & purification Protein Conformation receptors Receptors, Nicotinic - drug effects Receptors, Nicotinic - metabolism structure Torpedo Trypsin
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