Welcome to the Institute of Structural Biology!
The Institute of Structural Biology investigates the spatial structures of biological macromolecules (proteins, ribonucleic acids (RNAs) and their complexes) using state-of-the-art solution- and solid-state NMR-spectroscopy techniques as well as X-ray crystallography. Structural biology information obtained from these methods is combined with complementary data from Small Angle X-ray and/or Neutron Scattering (SAXS/SANS) and biophysical experiments (ITC, analytical ultracentrifugation) to describe the interplay between the structure and dynamics of biological macromolecules. We develop and improve new methodology to enable structural analysis of challenging systems by solid-state and solution-state NMR-spectroscopy.
The structural information provides an understanding of the molecular mechanisms of cellular pathways, including those linked to human disease. We investigate fundamental processes in the regulation of gene expression (pre-mRNA splicing, miRNA regulation, RNA localisation), cellular signal transduction and peroxisomal biogenesis. Our investigations provide a structural basis for the biological function of these molecules and thus for the molecular mechanisms of associated diseases, such as neurodegenerative disorders (Parkinson’s, Alzheimer’s, Fragile X-associated tremor/ataxia syndrome), diabetes and cancer. The structural data provide a rational basis for the design and development of small molecule inhibitors in combination with chemical biology approaches. Correspondingly, the institute plays an important role in the planned Munich Center for Bioactive Compound Research and Profiling.
The Protein Expression and Purification Facility (PEPF) has been established in 2010 to provide expertise and resources for sample preparation and producing proteins for structural studies, chemical biology and drug discovery.
In 2010 Bernd Reif was appointed as Professor of Solid-state NMR-Spectroscopy at the TU Munich and affiliated to the Institute of Structural Biology. With his expertise we can now study the structural basis of amyloids and amorphous/microcrystalline biological macromolecules, which play crucial roles in neurodegenerative diseases and diabetes.
Michael Sattler holds the Chair of Biomolecular NMR-Spectroscopy at the Technische Universität München TUM and is director of the Bayerische NMR Zentrum (BNMRZ), which is jointly supported by HMGU and TUM.
Research groups
1. Molecular recognition in the regulation of gene expression and signaling
Head: Michael Sattler (since 2007)
2. Solid-state NMR of amyloids and membrane proteins
Head: Bernd Reif (since 2010)
3. RNA localization and intracellular transport
Head: Dierk Niessing (since 2005)
4. Protein Expression and Purification Facility
Head: Arie Geerlof (since 2010)
Key publications
Mackereth CD, Madl T, Bonnal S, Simon B, Zanier K, Gasch A, Rybin V, Valcarcel J, and Sattler M
Multi-domain conformational selection underlies pre-mRNA splicing regulation by U2AF.
(2011) Nature 475, 408-11 [Pubmed]
[press release TUM][Pressemitteilung Helmholtz Zentrum München]
Müller M*, Heym R*, Mayer A, Kramer K, Schmid M, Cramer P, Urlaub H, Jansen RP, Niessing D
A cytoplasmic complex mediates specific mRNA recognition and localization in yeast.
(2011) PLoS Biol 9, e100611. *equal contribution
[Open Access] [Read Journal Highlight ] [Press Release (German)]
Simon B, Madl T, Mackereth CD, Nilges M, Sattler M.
An efficient protocol for NMR-based structure determination of protein complexes in solution.
(2010) Angew. Chem. Int. Ed. Engl. 49, 1967-70. [fulltext]; [press release]
Corsini L., Bonnal S., Basquin J., Hothorn M., Scheffzek K., Valcarcel J., and Sattler M. U2AF Homology Motif interactions are required for alternative splicing regulation by SPF45.
(2007) Nat Struct Mol Biol 14, 620-9. [PubMed]
Heuck, A., Du, T.-G., Jellbauer, S., Richter, K., Kruse, C., Jaklin, S., Müller, M., Buchner, J., Jansen, R.-P., and Niessing, D. Monomeric myosin V uses two binding regions for the assembly of stable translocation complexes.
(2007) Proc. Natl. Acad. Sci. USA - Track II: 105: 19778-19783. [PubMed]
Hantschel + O., Wiesner + S., Guttler T., Mackereth C.D., Rix L.L., Mikes Z., Dehne J., Gorlich D., Sattler* M., and Superti-Furga* G. Structural Basis for the Cytoskeletal Association of Bcr-Abl/c-Abl.
(2005) Mol. Cell 19, 461-73. [PubMed]
Niessing, D., Zenklusen, D., Hüttelmaier, S., Singer, R.H. and Burley, S.K. She2p is a Novel RNA-Binding Protein with a Basic Helical Hairpin Motif.
(2004) Cell 119: 491-502. [Pubmed]
Lingel A., Simon B., Izaurralde* E., and Sattler* M. Nucleic acid 3'-end recognition by the Argonaute2 PAZ domain.
(2004) Nat Struct Mol Biol 11, 576-7. [PubMed]
Lingel + A., Simon + B., Izaurralde* E., and Sattler* M. Structure and nucleic-acid binding of the Drosophila Argonaute 2 PAZ domain.
(2003) Nature 426, 465-9. [PubMed]
Liu + Z., Luyten + I., Bottomley M.J., Messias A.C., Houngninou-Molango S., Sprangers R., Zanier K., Krämer A., and Sattler M. Structural basis for recognition of the intron branch site RNA by splicing factor 1.
(2001) Science 294, 1098-102. [PubMed]
