The Ras dimer structure
Till Rudack, Christian Teuber, Marvin Scherlo, Jörn Güldenhaupt, Jonas Schartner, Mathias Lübben, Johann P. Klare, Klaus Gerwert, Carsten Kötting
Abstract
click chemistry. This labeling allowed the determination of multiple distances of the membrane-bound Ras-dimer measured by fluorescence and electron paramagnetic resonance spectroscopy. In combination with protein-protein docking and biomolecular simulations, we identified key residues for dimerization. Site-directed mutations of these residues prevent dimer formation in our experiments, proving our dimer model to be correct. The presented dimer structure enables computational drug-screening studies exploiting the Ras dimer interface as an alternative drug target.
Topics & Concepts
DimerMutagenesisChemistryAmino acidFörster resonance energy transferProtein structureBiophysicsBiochemistryMutationBiologyPhysicsGeneFluorescenceOrganic chemistryQuantum mechanicsProtein Structure and DynamicsElectron Spin Resonance StudiesEnzyme Structure and Function