Katharina Duerr

Membrane-embedded enzymes, receptors, channels and transporters are key regulators of essential cellular processes, such as metabolism, intercellular signalling and transport - making them prime targets for drug development. Despite their importance, structural information is limited, because membrane proteins are notoriously difficult to purify in large quantities and it is challenging to maintain their functional activity for structural studies.

The Membrane Protein Structure & Function (MPSF) group at the Structural Genomics Consortium (SGC) uses high-throughput screening methods to identify suitable candidates for structural studies from a large pool of human membrane proteins and their non-human homologues. After optimization of purification conditions in small-scale experiments and functional characterization, promising target proteins are produced in large quantities for structural studies, using X-ray crystallography or single-particle cryo-electron microscopy (cryo-EM). The molecular architecture determined by these methods can provide novel mechanistic insights into the function of membrane proteins and into their interactions with small molecule drugs, native ligands and substrates, and interacting proteins.