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© Marie Prévost, Institut Pasteur
Image of a portion of a Xenopus oocyte expressing a channel receptor.
Publication : The Journal of biological chemistry

Identification of a new component of the agonist binding site of the nicotinic alpha 7 homooligomeric receptor

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in The Journal of biological chemistry - 19 May 1995

Corringer PJ, Galzi JL, Eiselé JL, Bertrand S, Changeux JP, Bertrand D

Link to Pubmed [PMID] – 7744821

J. Biol. Chem. 1995 May;270(20):11749-52

Tryptophan 54 of the alpha 7 neuronal nicotinic homooligomeric receptor is homologous to gamma-Trp-55 and delta-Trp-57 of non-alpha subunits of Torpedo receptor labeled by d-tubocurarine. This residue was mutated on the alpha 7-V201-5-hydroxytryptamine (5HT)3 homooligomeric chimera, which displays alpha 7 nicotinic pharmacology, and for which both equilibrium binding studies and electrophysiological recordings could be carried out in parallel. Replacement of Trp-54 by a Phe, Ala, or His causes a progressive decrease both in binding affinity and in responses (EC50 or IC50) for acetylcholine, nicotine, and dihydro-beta-erythroidine, without significant modification in alpha-Bgtx binding. Except for Gln-56, comparatively small effects are observed when the other residues of the 52-58 region are mutated into alanine. These data support the participation of Trp-54 to ligand binding, and provide evidence for a new “complementary component” of the alpha 7 nicotinic binding site, distinct from its three-loop “principal component,” and homologous to the “non-alpha component” present on gamma and delta subunits.

http://www.ncbi.nlm.nih.gov/pubmed/7744821