The Dratz lab studies the structure and function of membrane receptor and amplifier proteins and uses global proteomic analysis to study signaling networks in cells. The mechanism of conversion of light to electrical signals in vision is of long-standing interest and is an archetype G protein-coupled receptor (GPCR) system that is responsible for over half the signaling systems in biology. Chemokine GPCRs that are responsible for intercellular signaling in the immune system are also used as receptors for virus entry. We are studying agonist and antagonist binding mechanisms in two chemokine receptors CCR5 and CXCR4 that AIDS virus uses to gain entry to lyphocytes and where infection is blocked by agonists and antagonists. Approaches include antibody imprinting for protein structure determination, development and application of new methods for global proteomics analysis, photochemical cross-linking of bioactive molecules to map out receptor binding sites, and protein and peptide mass spectrometry. In collaboration with Prof. Grieco's group we are developing new fluorescent dyes for ultrasensitive detection in proteomics and applying this technology for example, to new finding new diagnostic tools, to increased understanding of immune adjuvants and to understanding neurodevelopment. Prof. Dratz has a long standing interest in biochemical nutrition and is applying proteomic methods to gain deeper understanding of nutritional issues in collaboration with groups in Plant Sciences and Health and Human Nutrition.