ATOMIC RESOLUTION STUDY OF TRANSIENT STRUCTURES AND COMPLEXES OF MICROTUBULE ASSOCIATED PROTEIN 2c
Školitel: Dr. Lukas Zidek
Instituce: Masaryk University, CEITEC MU
Obor: Structural Biology
O mém projektu
Microtubule Associated Protein 2c (MAP2c), a intrinsically disordered protein important for development of nerve cells, expressed prenatally in dendrites. MAP2c shares high sequence homology of its C/terminal half with another ntrinsically disordered protein, Tau, which is studied intensively because its aggregates are found in brains of patients suffering from the Alzheimer's disease and the cognitive changes correlate with the Tau deposition. Dynamics, interactions, and structural features of MAP2c has been studied previously by this group. As the protein does not adopt a single structure, NMR was used to characterize its dynamics, interactions and transient structural features. The aim of the thesis is to use X-ray crystallography, and other relevant techniques to characterize with atomic resolution structures of MAP2c present in complexes with interacting partners and transiently in solution. X-ray crystallography will be used to determine crystal structures of the identified MAP2c fragments in complex with 14-3-3.