David B. Sauer

David Sauer is a biophysicist focusing on the structure and function of membrane channels and transporters. As group leader at the University of Oxford since 2021, he has been studying the structure and function of membrane proteins for 16 years. David completed his graduate degree studying potassium channel structure and ion selectivity with Youxing Jiang at the University of Texas Southwestern Medical Center. This was followed by postdoctoral training with Da-Neng Wang at New York University School of Medicine. There he described the structure, transport mechanism, and chemical inhibition of SLC13/DASS membrane transporters.

Since joining the Oxford's CMD, David had lead a group studying membrane proteins' function, pathogenesis, and chemical targeting by small molecules. This has resulted in the first detailed study of proline import by the transporter SIT1, and its complex with the SARS-CoV2 (COVID-19) receptor ACE2. His group has also revealed the ping-pong reaction mechanism, and product-bound inhibited state of the ceramide synthase CerS6. Finally, in a collaborative study, David's group revealed the substrate binding and transport triggers for SPNS2, which exports the immunoregulatory sphingosine-1-phosphate.