Structural Characterization of the Putative Cholinergic Binding Region alpha(179-201) of the Nicotinic Acetylcholine Receptor. Part 1. Review and Experimental Design.
Abstract
Because of the complex nature of the nicotinic acetylcholine receptor, it has not been possible to develop a reliable model of the cholinergic binding site. For example, the receptor has a molecular weight over 250,000 daltrons, five homologous subunits, and essential membrane bilayer. Small peptides of the region 170-210 of the a-subunit of the receptor have been shown to bind cholinergic agonist and competitive antagonist with binding profiles equivalent to the whole alpha-subunit and comparable to the whole solubilized receptor. It is likely that the folded structure of these peptides is similar to the folding of this region in vivo, and to some degree, is determined by the hydrophobic interaction of the residues within the relatively short region of a(170-210). By reducing the investigation primarily to this region, a considerably simpler model may provide a practical quantifiable model for understanding the underlying process of cholinergic binding at the molecular level. The research proposed investigates the structure of the putative cholinergic binding region of the nicotinic acetylcholine receptor and the contribution of the lipid bilayer membrane to cholinergic binding.
Document Details
- Document Type
- Technical Report
- Publication Date
- Apr 01, 1993
- Accession Number
- ADA266003
Entities
People
- James Vincent
- Jude Height
Organizations
- Edgewood Chemical Biological Center