NR ATQS
AU del Pino,P.; Weiss,A.; Mentler,M.; Renner,C.; Moroder,L.; Bertsch,U.; Kretzschmar,H.A.; Parak,F.G.
TI Characterisation of the Cu(II) Binding Sites in the N-Terminal Domain of the Prion Protein
QU International Conference - Prion 2005: Between fundamentals and society's needs - 19.10.-21.10.2005, Congress Center Düsseldorf - Poster Session: Structure of PrP and molecular determinants of infectivity STRCT-08
PT Konferenz-Poster
AB
Over the past few years, research work has demonstrated that the prion protein is a copper binding protein. Several studies have focused in the interaction of the prion protein with copper in the N-terminal domain of the protein, specifically in the octarepeat region, which consists of four tandem repeats of the sequence PHGGGWGQ.
A method for structure determination of metalloproteins that has been successfully applied to the Cu2+ complex of a single octapeptide repeat of the human prion protein is now used to infer the copper binding motifs of the tetraoctapeptid-Cu2 and the copper loaded PrPc.
This method combines molecular dynamics computations with spectroscopic data from extended X-ray absorption fine structure (EXAFS) electron paramagnetic resonance (EPR) and electron nuclear double resonance (ENDOR). Computations are used to select sterically possible structures which are sorted attending to certain restraints inferred from the spectroscopic data. The selected structures are analyzed by a 1H-ENDOR simulation program, which allows to compare computed spectra with the ENDOR spectra of the copper complex.
AD Pablo del Pino, Andreas Weiss, Matthias Mentler, Fritz G. Parak, Physik Department E17, Technische Universität München, 85747 Garching, Germany; Christian Renner, Louis Moroder, Laboratory of Bioorganic Chemistry, Max-Planck-Institut für Biochemie, 82152 Martinsried, Germany; Uwe Bertsch, Hans A. Kretzschmar, Zentrum für Neuropathologie und Prionforschung, LMU München, Germany
SP englisch
PO Deutschland