Dr. Michael Blanton - Faculty Page
Structure/Function of Ligand-Gated Ion Channels
LGIC: The nicotinic acetylcholine, serotonin (5-HT3), γ-aminobutyric acid type A (GABAA), and glycine receptors belong to a superfamily of ligand-gated ion channels (LGIC) each being critical for rapid signal transduction in the nervous system. In addition, each of these receptors constitute important target sites for many therapeutic drugs. Research in the lab is focused on two overall objectives: First, to determine how each of these ligand-gated ion channels function. More specifically, to identify and characterize the different structural elements, including the lipid-protein interface, that mediate each aspect of receptor function. To determine how each of these elements interact to effect the overall functioning of the receptor. Inclusive in this first goal is work aimed at determining in detail the structure of AChR functional elements (e.g. ion channel, lipid-protein interface. Secondly, to determine how drugs, in particular both local and general anesthetics (and neurosteroids), interact with each of the LGIC family members. Inclusive in this goal is not only understanding what are the determinants of drug binding but what are the mechanisms by which the binding of these ligands effect the structure of the receptor both locally as well as distally (i.e. allosterically). To accomplish these goals a wide array of techniques is employed in the laboratory and with collaborators, including: photoaffinity labeling, protein chemistry, spectroscopy (CD, FTIR, Fluorescence), as well as molecular biological and electrophysiological techniques.