Characterising the TSPO structure and ligand binding mechanism.
The translocator protein is an important outer mitochondrial membrane protein that facilitate cholesterol transport, oxidative stress sensing and apoptosis. We uses Nuclear Magnetic Resonance (NMR) spectroscopy, Electron Paramagnetic Resonance (EPR) spectroscopy and computational modelling to characterise the structure and ligand binding induced conformational changes of the protein.
Computational modelling to shed light on metabotropic glutamate receptors (mGluRs) signalling.
We employ a variety of computational ligand docking and protein-protein docking method in Rosetta to formulate hypothesis on how inter-domain signal transduction, receptor activation/inactivation in mGluRs based on published structure.
- Research Projects
Fei Li;Yan Xia, Jens Meiler, and Shelagh Ferguson-Miller
Characterization and Modeling of the Oligomeric State and Ligand Binding Behavior of Purified Translocator Protein 18 kDa from Rhodobacter sphaeroides (2013) ACS Biochemistry
Huixian Wu;Chong Wang, Karen J. Gregory, Gye Won Han, Hyekyung P. Cho, Yan Xia, Colleen M. Niswender, Vsevolod Katritch, Jens Meiler, Vadim Cherezov, P. Jeffrey Conn, Raymond C. Stevens
Structure of a Class C GPCR Metabotropic Glutamate Receptor 1 Bound to an Allosteric Modulator (2014) Science