Nicotinic Receptor Binding Site Probed with Unnatural Amino Acid Incorporation in Intact Cells.
Abstract
In the study of membrane-bound receptor, channel, and transporter proteins, classical pharmacology has defined highly specific agonists and antagonists; and quantitative structure-activity studies have generated many hypotheses concerning ligand-receptor interactions. More recently, the combination of site-directed mutagenesis and heterologous expression has enabled functional studies on the consequences of structural modifications of the receptors. In the absence of atomic-scale structural data for membrane-bound receptors, these methods provide detailed information for studying ligand-receptor interactions. First generation mutagenesis methodologies employed the normal translation machinery such that a residue of interest could be changed to any of the other 19 natural amino acids.
Document Details
- Document Type
- Technical Report
- Publication Date
- Feb 01, 1995
- Accession Number
- ADA299991
Entities
People
- Henry A. Lester
Organizations
- California Institute of Technology