NDLI: Two subsites in the binding domain of the acetylcholine receptor: an aromatic subsite and a proline subsite.

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Two subsites in the binding domain of the acetylcholine receptor: an aromatic subsite and a proline subsite.

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Two subsites in the binding domain of the acetylcholine receptor: an aromatic subsite and a proline subsite.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Kachalsky, S. G. Barchan, D. Jensen, B. S. Fuchs, S.
Description	Author Affiliation: Kachalsky SG ( Department of Chemical Immunology, Weizmann Institute of Science, Rehovot, Israel.);
Abstract	The ligand binding site of the nicotinic acetylcholine receptor (AcChoR) is localized in the alpha-subunit within a domain containing the tandem Cys-192 and -193. By analyzing the binding-site region of AcChoR from animal species that are resistant to alpha-neurotoxins, we have previously shown that four residues in this region, at positions 187, 189, 194, and 197, differ between animals sensitive (e.g., mouse) and resistant (e.g., mongoose and snake) to alpha-bungarotoxin (alpha-BTX). In the present study, we performed site-directed mutagenesis on a fragment of the mongoose AcChoR alpha-subunit (residues 122-205) and exchanged residues 187, 189, 194, and 197, either alone or in combination, with those present in the mouse alpha-subunit sequence. Only the mongoose fragment in which all four residues were mutated to the mouse ones exhibited alpha-BTX binding similar to that of the mouse fragment. The mongoose double mutation in which Leu-194 and His-197 were replaced with proline residues, which are present at these positions in the mouse AcChoR and in all other toxin binders, bound alpha-BTX to approximately 60% of the level of binding exhibited by the mouse fragment. In addition, replacement of either Pro-194 or -197 in the mouse fragment with serine and histidine, respectively, markedly decreased alpha-BTX binding. All other mutations resulted in no or just a small increase in alpha-BTX binding. These results have led us to propose two subsites in the binding domain for alpha-BTX: the proline subsite, which includes Pro-194 and -197 and is critical for alpha-BTX binding, and the aromatic subsite, which includes amino acid residues 187 and 189 and determines the extent of alpha-BTX binding.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	23
Volume Number	92
Language	English
Publisher	National Academy of Sciences
Publisher Date	1995-12-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Bungarotoxins Metabolism Nicotinic Antagonists Receptors, Nicotinic Amino Acid Sequence Animals Binding Sites Genetics DNA Mutational Analysis Drug Resistance Herpestidae Mice Molecular Sequence Data Mutagenesis, Site-Directed Peptide Fragments Pharmacology Sequence Homology, Amino Acid Species Specificity Structure-Activity Relationship Comparative Study Research Support, Non-U.S. Gov't Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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