Accession Number : ADA299991

Title :   Nicotinic Receptor Binding Site Probed with Unnatural Amino Acid Incorporation in Intact Cells.

Descriptive Note : Final technical rept.,

Corporate Author : CALIFORNIA INST OF TECH PASADENA DIV OF BIOLOGY

Personal Author(s) : Lester, Henry A.

PDF Url : ADA299991

Report Date : 01 FEB 1995

Pagination or Media Count : 24

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.

Descriptors :   *CELLS(BIOLOGY), *AMINO ACIDS, *NICOTINIC ACID, METHODOLOGY, CARGO VEHICLES, MEMBRANES(BIOLOGY), INTERACTIONS, STRUCTURAL PROPERTIES, PROTEINS, MUTATIONS, MACHINES, TRANSLATIONS, HYPOTHESES, SENSE ORGANS, PHARMACOLOGY.

Subject Categories : Medicine and Medical Research
      Biochemistry

Distribution Statement : APPROVED FOR PUBLIC RELEASE