Christos Gatsogiannis

Christos Gatsogiannis

Project Group Leader, Structural Biochemistry


Research Projects

Pore-forming Proteins

Pore-forming proteins represent a unique class of highly specific lipid-binding proteins, which undergo a sophisticated metamorphosis from a soluble prepore, to a transmembrane pore state. We are especially interested to understand the underlying mechanisms of those pore-forming proteins that are capable to insert into membranes, in a regulated manner.

Peroxisomal protein import pore

The import of natively folded proteins into the peroxisomal matrix is directed by specific targeting signals. Cargo-proteins are imported via binding to a cytosolic receptor, which undergoes a conformation change and becomes an integral component of a transient import pore. So far structures of the import pores, needed to understand the translocation mechanism, are missing. Our lab is dedicated to elucidate the 3D- structure of the peroxisomal translocation pores, facilitating the PTS1- and PTS2-dependent protein import into the organellar matrix.

Protein origami: the structure of molluscan hemocyanin

Animals have a continuous need for oxygen to sustain an efficient aerobic metabolism and produce sufficient amounts of ATP. In most mollusks, the crucial role of oxygen transport in the hemolymph is facilitated by the blue respiratory pigment hemocyanin. Hemocyanins from gastropods, i.e., snails and slugs, have received particular interest because of their remarkable immunological properties in laboratory animals and man. A prominent example is keyhole limpet hemocyanin (KLH), which is widely used in medical research and clinical studies as vaccine carrier and as immunotherapeutical agent for the treatment of bladder carcinomas. We use cryoEM and modeling techniques to provide a detailed molecular picture of the complex macromolecular machines and understand their evolution, structure and function.

Method Development

The development of novel reagents, including nanodiscs and amphipols, has greatly facilitated functional and structural studies of integral membrane proteins (IMPs). We are interested in developing novel and delicate methodologies with the help of the DNA-origami technology, to optimize the sample quality of IMPs for high-resolution structural analysis by cryoEM.

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