The International Max Planck Research School for Chemical and Molecular Biology (IMPRS-CMB) is a collaboration between the Max Planck Institute of Molecular Physiology and three universities, the Technical University Dortmund (TU Dortmund), the Ruhr University Bochum (RUB) and the University of Duisburg-Essen (DUE).

All four institutes are located in the Ruhr Metropolitan Area of Germany, an extremely vibrant and culturally interconnected region. The same spirit is reflected in the science of our program: research groups, with different and often complementary approaches, combine their efforts to study at the molecular level basic cell physiology.

Below you can find all the research groups that are part of IMPRS-CMB, in alphabetical order. You can also search groups by name, topic or technique.

Read about OUR SCIENCE by visiting the webpages of our Faculty Members.

ingrid foto-webCRYSTALLOGRAPHY

Dr. Ingrid Vetter

Current Position: Group Leader Crystallography, MPI Dortmund
Postdoc: EMBL Heidelberg, Germany (Dimitri Tsernoglou), University of Oregon, Eugene, OR, USA (Brian Matthews)
PhD: MPI of medical Research, Heidelberg, Germany (Paul Rösch, Ken Holmes)

Research Interest
Crystallography of disease-relevant proteins
We investigate the structure and biochemical/biophysical properties of disease-relevant proteins with a focus on small GTPases and their binding partners. Especially the dynamic properties of the oncogene Ras and the structure and properties of the Ras-regulators acyl protein thioesterases that are involved in the lipid modification of Ras proteins are in the focus of our group. We apply molecular modeling and bioinformatics tools to aid the design and optimization of small molecule inhibitors that are used in our structural studies.

Crystallography, Bioinformatics, Molecular Modelling, Docking, Drug Design, Molecular Biology, Protein Purification, Biochemistry, Biophysical Methods

Selected Reading
Bürger M, Zimmermann TJ, Kondoh Y, Stege P, Watanabe N, Osada H, Waldmann H, Vetter IR. Crystal structure of the predicted phospholipase LYPLAL1 reveals unexpected functional plasticity in spite of close relationship to acyl protein thioesterases. J Lipid Res 2012, 53, 43-50.

Wittinghofer A and Vetter IR. Structure-function relationships of the G domain, a canonical switch motif. Annu Rev Biochem 2011, 80, 943-971.

Schrader N, Koerner C, Koessmeier K, Bangert JA, Wittinghofer A, Stoll R, Vetter IR. The crystal structure of the Ran-Nup153 complex: A General Ran docking site at the nuclear pore complex. Structure 2008, 16, 1116-1125.

Schrader N, Stelter P, Flemming D, Kunze R, Hurt E, Vetter IR. Structural basis of the Nic96 subcomplex organization in the nuclear pore channel. Mol Cell 2008, 29, 46-55.

Sarić M, Zhao X, Körner C, Nowak C, Kuhlmann J, Vetter IR. Structural and biochemical characterization of the Importin-beta.Ran.GTP.RanBD1 complex. FEBS Lett 2007, 581, 1369-1376.

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