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Joint Project
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Cu(II) binding of cellular prion protein PrPC:
influence on structure and conformational dynamics
A joint project within the Bayerische Forschungsverbund Prionforschung by Paul Tavan (speaker of the joint project, Theoretical Biophysics, LMU), Hans Kretzschmar (Institute for Neuropathology, LMU), Luis Moroder (MPI for Biochemistry, Bioorganic Chemistry, Martinsried), Fritz Parak (Experimental Physics, Biophysics, TUM). The lack of knowledge about the complete three-dimensional structure of PrPC is a severe obstacle for the deeper understanding of prion diseases. Our joint project, with its goal to gain detailed information on the structure of human PrPC, relies on the expertise of four research groups working in different disciplines that cover neuropathology, bioorganic chemistry, experimental and theoretical biophysics. The objective of this study is the understanding of refolding and aggregation of PrPC into the infectious form PrPSC. In summary the research project will focus on -the nature and selectivity of Cu(II) binding by PrPC, -the structural effects associated with Cu(II) binding to PrPC, -the possible role of Cu(II) binding and/or membrane environment in the conformational transitions that lead to PrPSC, i.e. to protein aggregation/oligomerization and infectivity. |
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Letzte Änderung: Letzte Änderung: 1970-01-01 01:00
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