The protein crystallography group of Ute Krengel uses X-ray crystallography to determine the molecular structures of proteins at atomic resolution.The main focus is on proteins of medical interest and in particular on protein-carbohydrate interactions.
- KJM2200 - Biological Chemistry
- KJM4350 - Protein crystallography
- KJM5310 - Biomolecular Structure and Function
- KJM9310 - BIOSTRUCT - Biomolecular structure and function
- MBV4270 - BIOSTRUCT - Advanced Glycobiology
English-Norwegian word list for biochemical terms
Significance of the Scientific Problem and Potential Applications
Protein-carbohydrate interactions are central to many biological processes (e.g. cell-cell interaction, cellular signaling and differentiation, immune response) that are at the core of important diseases. Understanding the roles of carbohydrates in these processes and how they interact with proteins is expected to have a large impact on the development of new treatments against many human diseases.
The work involves the close collaboration with research groups of different specializations (e.g.biochemists, molecular modelers, bioinformaticians, NMR and mass spectrometrists), thus warranting that the structural characterization of the chosen research targets can be pursued hand in hand with protein engineering and carbohydrate binding studies, microcalorimetry and molecular modeling.
Main targets currently under investigation
Legume and mushroom lectins, adhesins, toxins, mucins, and anti-cancer antibodies.
Review series: Nature 2007, 446, 999-1051 and Science 2001, 291, 2337-2378.
U. Krengel & A. Imberty (2007), Crystallography and lectin structure database, In: Lectins: Analytical technologies (C. Nilsson, Ed.), Elsevier, 15-50.
G. Cordara & U. Krengel (2013). Lectin structure determination by X-ray crystallography – A hands-on approach. In: SPR Carbohydrate Chemistry Vol 39 (A. Rauter, Ed.), RSC, 222-246.
A. van Eerde, E.M. Grahn, H.C. Winter, I.J. Goldstein & U. Krengel (2015). Atomic-resolution structure of the α-galactosyl binding Lyophyllum decastes lectin reveals a new protein family found in both fungi and plants. Glycobiology 25, 492-501.
Å. Holmner, A. Mackenzie & U. Krengel (2010). Hypothesis: Molecular basis of cholera blood-group dependence and implications for a world characterized by climate change. FEBS Lett. 584, 2548-2555.
U. Krengel & P.A. Bousquet (2014). Molecular recognition of gangliosides and their potential for cancer immunotherapies. Front Immunol. 5, 325, 1-11.
D. Burschowsky, A. van Eerde, M. Ökvist, A. Kienhöfer, P. Kast, D. Hilvert & U. Krengel (2014) .Electrostatic transition state stabilization rather than reactant destabilization provides the chemical basis for efficient chorismate mutase catalysis. Proc Natl Acad Sci U S A. 111, 17516-21.
U. Krengel & S. Törnroth-Horsefield (2015). Coping with oxidative stress. Science 347, 125-6.