Hagn Lab
We work on biologically important systems, such as mitochondrial membrane proteins, G-protein coupled receptors (GPCRs) and their associated G-proteins and metabolite transporters in plants. These membrane proteins are involved in metabolic diseases, neurological disorders and cancer, or supply energy to enable plant growth and the generation of biomass. Beside NMR, we use electron microscopy, X-ray crystallography and a variety of other biophysical, biochemical and computational methods.
We work on biologically important systems, such as mitochondrial membrane proteins, G-protein coupled receptors (GPCRs) and their associated G-proteins and metabolite transporters in plants. These membrane proteins are involved in metabolic diseases, neurological disorders and cancer, or supply energy to enable plant growth and the generation of biomass. Beside NMR, we use electron microscopy, X-ray crystallography and a variety of other biophysical, biochemical and computational methods.
About us
Membrane proteins are essential for signal transduction and the transfer of proteins and small molecules across the biological membrane barrier and thus represent around 60% of current drug targets. We aim at characterizing the structure, dynamics, small molecule and partner protein interactions of selected membrane protein systems to obtain essential insights on their functionality and to facilitate rational drug design approaches.
Our main tool to achieve this goal is nuclear magnetic resonance (NMR) spectroscopy. In order to be able to study membrane proteins in a native lipid environment we develop novel and advanced membrane mimetics, called phospholipid nanodiscs, for their use in biochemical, biophysical and structural studies.
We work on biologically important systems, such as mitochondrial membrane proteins, G-protein coupled receptors (GPCRs) and their associated G-proteins and metabolite transporters in plants. These membrane proteins are involved in metabolic diseases, neurological disorders and cancer, or supply energy to enable plant growth and the generation of biomass. Beside NMR, we use electron microscopy, X-ray crystallography and a variety of other biophysical, biochemical and computational methods.
Group members
Postdoc
PhD student
PhD student
PhD student
Technical assistant
Assistant to Prof. Hagn
PhD student
Publications
Daniilidis, M. ; Günsel, U. ; Broutzakis, G. ; Leitl, K.D. ; Janowski, R. ; Fredriksen, K. ; Niessing, D. ; Gatsogiannis, C. ; Hagn, F.
Structural basis of apoptosis induction by the mitochondrial voltage-dependent anion channel.Kogut-Günthel, M.M. ; Zara, Z. ; Nicoli, A. ; Steuer, A. ; Lopez-Balastegui, M. ; Selent, J. ; Karanth, S. ; Koehler, M. ; Ciancetta, A. ; Abiko, L.A. ; Hagn, F. ; Di Pizio, A.
The path to the G protein-coupled receptor structural landscape: Major milestones and future directions.Leitl, K. ; Sperl, L.E. ; Hagn, F.
Preferred inhibition of pro-apoptotic Bak by BclxL via a two-step mechanism.Daniilidis, M. ; Sperl, L.E. ; Müller, B.S. ; Babl, A. ; Hagn, F.
Efficient segmental isotope labeling of integral membrane proteins for high-resolution NMR studies.Günsel, U. ; Klöpfer, K. ; Häusler, E. ; Hitzenberger, M. ; Bölter, B. ; Sperl, L.E. ; Zacharias, M. ; Soll, J. ; Hagn, F.
Structural basis of metabolite transport by the chloroplast outer envelope channel OEP21.Hagn Lab Contact