Institute of Structural Biology
University of Bonn

Welcome to our Institute!  We are interested in the structure–function relationship of biological macromolecules.  We use molecular biology techniques, biochemistry, biophysics, X-ray crystallography and cryo electron microscopy to investigate biological phenomena at atomic resolution.  

In today’s issue of Nature, Matthias and Gregor wrote a News & Views piece on the cryo-EM structures of cytoplasmic lattices (CPLs). Early embryonic development, when the embryonic genome is still silenced, relies on preassembled complexes that store and protect proteins. The CPL filament consists of repeating units, each composed of at least 63 subunits from 16 different proteins, with a molecular mass of approximately 4 MDa. Three studies now provide fascinating insights into the function and architecture of this maternal storage system. Read the full story here....

The P2X4 receptor is a promising drug target linked to chronic pain, inflammation, and cancer. Together with the team of Christa Muller from the Pharmaceutical Institute, Gregor uncovered a novel allosteric binding site in P2X4 where anthraquinone compounds selectively block receptor activity. A tiny structural feature, an “ionic lock,” controls how strongly these molecules bind, opening the door to dramatically more potent inhibitors. The study provides a high-resolution structural blueprint for designing next-generation therapeutics for inflammatory and neurological diseases. Read the full story here......

Together with Sneha Singh, Arijit Biswas and Johannes Oldenburg from the Institute of Hematology, Gregor and Matthias determined the first structure of the A and B subunits of Factor XIII. This tetrameric protein complex plays an important role in blood coagulation and is linked to many bleeding disorders. Using single particle cryo-EM, we were able to resolve the FXIII-A2B2 complex at 2.4 Å resolution. Read all about this exciting story here....
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