Expertise
The group of Titia Sixma uses a combination of structural, biochemical and biophysical techniques to study protein function at the molecular level. These data, combining structure with functional insight will improve understanding of fundamental processes and create a basis for structure assisted drug design. The Netherlands Cancer Institute (NKI) is an integrated cancer center with excellent facilities for advanced cell biology, including state of the art transgenic mouse facility, confocal microscopy, live-cell imaging, DNA microarray technology, immuno-EM, biophysics, high-through-put screening and structural biology.
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Selected references
- Lebbink, J.H.G, Georgijevic, D., Natrajan, G., Fish, A., Winterwerp, H.H.K., Sixma, T.K., de Wind, N. Dual roles of MutS glutamate 38 in DNA mismatch discrimination and in the authorization of repair. EMBO J 2006 25:409-419
- Lamers, M.H., Georgijevic, D., Lebbink, J.H., Winterwerp, H.H., Agianian, B., De Wind, N., Sixma, T.K. ATP increases the affinity between MutS ATPase domains; Implications for ATP hydrolysis and conformational changes. J Biol Chem 2004 279:43879-43885
- Natrajan, G., Lamers, M.H., Enzlin, J.H., Winterwerp, H.H.K., Perrakis, A., Sixma, T.K. Structures of Escherichia coli DNA mismatch repair enzyme MutS in complex with different mismatches: a common recognition mode for diverse substrates Nucl Acids Res 2003 31:4814-4821
- Lamers, M.H., Winterwerp H.H.K., Sixma, T.K. The alternating ATPase domains of the DNA mismatch repair enzyme MutS control DNA mismatch repair. EMBO J 2003 22:746-756
- Lamers, M.H., Perrakis, A., Enzlin, J.H., Winterwerp, H.H.K., de Wind, N., Sixma, T.K. The crystal structure of DNA mismatch repair protein MutS binding to a G:T mismatch. Nature 2000 407:711-717.
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