Methods in Protein Sequence Analysis
Brigitte Wittmann-Liebold
- 01 Jan 1989
309
TL;DR: The AChR-binding sites on a-bungarotoxin by synthetic peptides representing the exposed regions of each of the toxin loops are localized by synthetic Peptide size selected to be within the optimum size requirement for T-cell activation.
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Abstract: A comprehensive synthetic approach, previously developed in this laboratory, has been applied to systematically screen the entire extracellular part (residues 1-210) of the a subunit of human and Torpedo californica acetylcholine receptors (AChR) for the various functional sites. Consecutive uniform-sized peptides were designed with constant 5-residue overlaps and covered the entire extracellular domain (residue 1-210) of I. californica and human AChR a subunits. The peptide size was selected to be within the optimum size requirement for T-cell activation. These pept i des were employed to 1 oca 1 i ze the cont i nuous regions recogni zed by anti-AChR antibodies, the regions recognized by AChR-primed T-lymphocytes and the regions that are involved in the binding of a-neurotoxins and of acetylcholine. We have also synthesized the two inter-transmembrane regions a262-276 and a-388408 as well as the f-terminal segment a427-437 and have determined their ability to bind a-neurotoxins (BgTX and CbTX) and antibodies against free AChR and membrane-bound AChR and to stimul ate the ~ vitro pro 1 i ferat i on of AChR-primed T-lymphocytes. This permitted the selection of a model for subunit organization within the membrane. In addition, we have also localized the AChR-binding sites on a-bungarotoxin by synthetic peptides representing the exposed regions of each of the toxin loops.
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