Functional Characterization of Odorant Receptors
Abstract
Our studies on the functional characterization of odorant receptors have developed in two directions. One direction is concerned with the characterization of the ligand specificity of a single defined odorant binding domain. The fourth and fifth transmembrane domains and their extracellular linker of the human beta (2)-adrenergic receptor have been replaced by the equivalent regions of odorant receptor I-15 (Buck and Axel, 1991), thus forming a chimaeric seven transmembrane domain containing G-protein linked receptor that couples a novel odorant binding domain consisting of the 1-15 moiety (and perhaps part of the adrenaline binding site of the adrenergic receptor) to the intracellular regions of the Beta (2)-adrenergic receptor that couples ligand binding to the production of cyclic AMP. Expression of this chimaera in eukaryotic cells and screening the expressed construct with an array of odorants is expected to identify a set of odorants that interacts with the ligand binding domain of the synthetic receptor. The binding site can then be characterized pharmacologically and the interactions of odorants with specific amino acid residues in the hybrid receptor can be studied. This information can then be used to characterize the odorant specificity of the parental 1-15 receptor, that may not be identical, but is likely to be closely related to that of the chimaera. The second direction of our research program is concerned with the question of how an ensemble of odorant receptors with overlapping ligand specificities interacts to recognize a given odorant.
Document Details
- Document Type
- Technical Report
- Publication Date
- Feb 07, 1994
- Accession Number
- ADA276118
Entities
People
- Robert R. Anholt
Organizations
- Duke University Hospital