Max Planck Research Unit for Structural Molecular Biology at DESY

Max Planck Research Unit for Structural Molecular Biology at DESY

Proteins are folded into three-dimensional structures and modify their spatial arrangement dynamically in the course of biological reactions. The structural and functional relationships between proteins, multi-protein systems and the protein fibres in the cytoskeleton (microtubules) are examined in atomic detail at the Max Planck Research Unit for Structural Molecular Biology in Hamburg. X-ray crystal structure analysis is carried out using highly intensive synchrotron radiation sources at the Deutsches Elektronensynchrotron (DESY, German Electron Synchrotron). The scientists seek to explain, among other things, the role played by the tau protein in the emergence of Alzheimer’s disease. They also examine proteins from the tuberculosis bacterium to find starting points for the discovery of active agents to treat this disease. A large part of the research of Ada Yonath, who was awarded the Nobel Prize in chemistry in 2009, was carried out at this research unit. Here, she decoded the structure of ribosomes, the cell’s protein factories, and thus facilitated the search for innovative antibiotics.

The Max Planck Research Unit for Structural Molecular Biology at DESY was closed in July 2011.

Contact

Notkestr. 85
22607 Hamburg
Phone: +49 40 8998-2801
Fax: +49 40 897168-10

PhD opportunities

This institute has no International Max Planck Research School (IMPRS).

There is always the possibility to do a PhD. Please contact the directors or research group leaders at the Institute.

Tau-induced memory loss in Alzheimer’s mice is reversible
Max Planck study raises hopes for the development of effective therapies more
"Associated with the Max Planck Society for more than 20 years"
President Peter Gruss congratulates the former senior research scientist Ada E. Yonath on winning the 2009 Nobel Prize for Chemistry more
Forgotten and lost - when proteins "shut down" our brain
Scientists obtained important insights into the structure and interaction of a protein relevant to Alzheimer’s disease more

Reversible tau pathology in mice

2011 Mandelkow, Eckhard
Medicine Neurosciences Structural Biology
Microtubules are protein fibres that are essential for determining the cells' shape, for cellular motion and cell division. In Alzheimer's disease, the microtubule-associated Tau protein, which is normally bound to the microtubule surface, forms characteristic aggregates in nerve cells. Transgenic cell and mouse models showed that the loss of synapses and neurons in Alzheimer's disease correlates with the aggregation of Tau. The concomitant impairment of learning and memory in mice can be reversed by suppression of Tau aggregation. more
The soil bacterium Arthrobacter nicotinovorans grows on nicotine. Degradation of L-nicotine and D-nicotine involves two genetically unrelated flavoenzymes, 6HLNO and 6HDNO. Their crystal structures may explain the stereospecificity of their enzymatic reactions. 6HLNO by its structure and mechanism is closely related to human monoamine oxidases (MAO), which play central roles in degradation of neurotransmitters. Structural analysis of 6HLNO reaction intermediates and the inhibition mechanism extends the basis for possible development of new leads for MAO. more

Cytoskeleton: Architecture and movement of cells

2009 Mandelkow, Eckhard
Medicine Neurosciences Structural Biology
The "Cytoskeleton" group of the Max Planck Unit for Structural Molecular Biology in Hamburg focuses on the structure and dynamics of protein fibers in cells, in particular on microtubules and their associated proteins which are responsible for cell movement, cell division, or intracellular transport. One of these proteins, tau, forms pathological aggregates in nerve cells affected by Alzheimer's disease. Recent transgenic cell and mouse models of the tau pathology reveal that the pathological degeneration of synapses and neurons is closely related to aggregation, and that it is reversible. more
Tuberculosis represents a global health threat of escalating proportions, in particular due to the emergence of multi-drug resistant strains. Furthermore, little is known about the mechanisms applied by Mycobacterium tuberculosis to enter a dormant state, thus resisting to the immune defense system over long periods of time, and to reactivate itself. Identification of genes that are essential for virulence and survival of the pathogen, analysis of the three-dimensional structure of proteins encoded by these genes and studies of interactions with ligands may provide an important basis for possible directed development of new chemotherapeutic agents. Such a structural genomics approach has been followed by several groups and up to now have investigated about 200 target proteins. more

Cytoskeleton: Architecture and movement of cells

2007 Mandelkow, Eckhard
Medicine Neurosciences
The "Max-Planck-Unit for Structural Molecular Biology" in Hamburg investigates the structure and function of biomolecules, with particular emphasis on the applications of synchrotron radiation for the elucidation of protein structures of biomedical interest. The "Cytoskeleton" group focuses on the structure, self-assembly, and dynamics of protein fibers in cells, in particular on microtubules and their associated proteins which are responsible for cell movement, cell division, cell differentiation, or intracellular transport. One of the microtubule associated proteins, tau protein, forms pathological aggregates in nerve cells affected by Alzheimer's disease. Recent findings reveal a linkage between tau's multiple functions and the cellular transport system which could prove essential for the aetiology of Alzheimer's disease. more
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