The Cholinergic Binding Site: From Sequence to Function
Whereas the sequence of the nicotinic acetylcholine receptor (AChR) has been known since 1983 (Numa et al 1983), a true understanding of how this receptor functions is far from clear. In fact, this situation is quite characteristic of much of today’s molecular biology. The purification of a given protein is readily feasible, N-terminal sequencing has been impressively perfected and the subsequent steps for cloning the desired protein and the’ generation of a postulated sequence have become almost routine. Yet strategies, which allow the efficient correlation between sequence and function, are still being developed and few have been proven effective.
KeywordsAcetylcholine Receptor Nicotinic Acetylcholine Receptor Ligand Recognition Oligosaccharide Side Chain Crude Membrane Preparation
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- Aronheim A, Eshel Y, Mosckovitz R, Gershoni JM (1988) Characterization of the binding of oc -bungarotoxin to bacterially expressed cholinergic binding sites. J Biol Chem 263: in pressGoogle Scholar
- Fraenkel Y, Navon G, Aronheim A, Gershoni JM (1988) Selective and non-selective Tl measurements of binding constants of acetylcholine and its antagonists to synthetic and genetically engineered peptides of the acetylcholine receptor. 13th Int Conf Magnetic Resonance in Biological Systems. 14–19 August, Madison, WisconsinGoogle Scholar
- Gershoni JM, Aronheim A (1988) Molecular decoys: ligand-binding recombinant proteins protect mice from curarimimetic neurotoxins. Proc Natl Acad Sci USA 85: in pressGoogle Scholar
- Karlin A (1980) Molecular properties of nicotinic acetylcholine receptors. In: Cotman CW, Poste G, Nicolson GL (eds) The Cell Surface and Neuronal Function. Elsevier/North Holland Biomedical, Amsterdam, pp 192–260Google Scholar