NR AURU
AU Ziegler,J.; Einsiedel,J.; Gmeiner,P.; Schwarzinger,S.
TI Binding of the 37/67 kDa LRP to PrP studied by NMR
QU TSE-Forum, 6. Kongress - Nationale TSE-Forschungsplattform, Greifswald 26.6.-28.6.2006, Poster: Struktur und molekulare Mechanismen MOL-18
PT Konferenz-Poster
AB The 37/67 kDa laminin receptor precursor (LRP) protein was reported to bind to the prion protein and to be a promising candidate for anti-prion therapy. However, no structrual data - neither on isolated LRP nor on its complex with the prion protein - are presently available. We have expressed the C-terminal domain of LRP(102-295) in high yield for solution NMR-studies. Using a newly developted screening system we show that the LRP binds to the prion protein under NMR-conditions. Hence, NMR appears a suitable technique to study the structural interaction of these two proteins. We further present first low resolution structural data on the binding of the PrP-binding domain from LRP (161-179) to 15N-labeled prion protein using paramagnetic probes covalently attached to the LRP-peptide.
AD Jan Ziegler und Stephan Schwarzinger, Lehrstuhl Biopolymere, Universität Bayreuth, Universitätsstrasse 30, 95440 Bayreuth; Einsiedel,J. und Gmeiner,P. Lehrstuhl medizinische Chemie, Friedrich-Alexander-Universität Erlangen
SP englisch
PO Deutschland
EA Photo des Posters, welches nach Auskunft von S. Schwarzinger korrekterweise statt der im Tagungsband genannten Coautoren Stephan Pischel, Christian Mangels und Birgitta M. Wöhrl die Coautoren Einsiedel,J. und Gmeiner,P. nennt
OR Tagungsband