Cookies on this website

We use cookies to ensure that we give you the best experience on our website. If you click 'Accept all cookies' we'll assume that you are happy to receive all cookies and you won't see this message again. If you click 'Reject all non-essential cookies' only necessary cookies providing core functionality such as security, network management, and accessibility will be enabled. Click 'Find out more' for information on how to change your cookie settings.

Understanding the mechanisms of membrane enzymes, their mechanism of pathogenesis, and enabling their targeting by new therapeutics.

Graphical abstract of Sauer group. Left: Substrate binding by SPNS2. Right: Acylated histidine and ping-pong reaction mechanism of CerS6.

Lipid membranes are a chemical and physical barrier which separate the inside and outside of a cell and its organelles. Membrane proteins are therefore required for fundamental import nutrients, export waste, and transmit information within and between cells. Accordingly, these proteins are often mutated in disease and targeted by therapeutic drugs.

Our aim is to examine the biochemistry and determine atomic structures to describe the link between these proteins’ structure and function. To do so we work with scientific colleagues around the globe, developing tools to probe membrane proteins’ roles in human physiology. Through these results we will explain pathophysiology of toxins and mutations, validate these proteins as therapeutic targets, and develop new drugs to treat a variety of diseases.

Recently, our efforts have yielded the first detailed study of proline import by the transporter SIT1, and its complex with the SARS-CoV2 (COVID-19) receptor ACE2. We have also revealed the ping-pong reaction mechanism, and product-bound inhibited state of the ceramide synthase CerS6. Finally, in a collaborative study, our group revealed the substrate binding and transport triggers for SPNS2, which exports the immunoregulatory sphingosine-1-phosphate and the multiple sclerosis drug Fingolimod.

We have collaborations with academic and industrial partners worldwide. Our work is funded by several IMI consortia, pharma collaborators, the BBSRC and the MRC, the Royal Society, and the Macular Society.

Our team

  • David Sauer
    David Sauer

    Principal Investigator, Membrane Protein Structural and Chemical Biology

  • Gamma Chi
    Gamma Chi

    Senior Scientist in Rare Diseases and Structural Biology

  • Ashley Pike
    Ashley Pike

    Senior Scientist

  • Roslin Adamson

    Postdoctoral Scientist - Membrane Protein Structure and function group

  • David Speedman

    DPhil Student - Membrane Protein Structure and Function group

  • Huanyu Li

    Postdoctoral Scientist - Membrane Protein Structure and function group

  • Anna Li
    Anna Li

    DPhil Student - Membrane Protein Structure and Function group

  • Matthew Hankins

    DPhil Student - Membrane Protein Structure and Function group

  • Mingda Ye

    Postdoctoral Scientist - Membrane Protein Structure and function group

  • Vijay Kumar

    Postdoctoral Scientist - Membrane Protein Structure and function group