Abstract
Prion diseases are invariably fatal and highly infectious neurodegenerative diseases that affect humans and animals. Rabbits are the known mammalian species reported to be resistant to infection from prion diseases isolated from other species (Vorberg et al., J Virol 77(3):2003–2009, 2003). Fortunately, the NMR structure of rabbit prion protein (124–228) (PDB entry 2FJ3), the NMR structure of rabbit prion protein mutation S173N (PDB entry 2JOH) and the NMR structure of rabbit prion protein mutation I214V (PDB entry 2JOM) were released recently (Wen et al., J Biol Chem 285(41):31682–31693, 2010; PLoS ONE 5(10):e13273, 2010). This chapter studies these NMR structures by MD simulations. Simulation results confirm the structural stability of wild-type rabbit prion protein , and show that the SB D177-R163 greatly contributes to the structural stability of rabbit prion protein.
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Zhang, J. (2015). The NMR Structure and Dynamics of the Wild-Type and Mutants. In: Molecular Structures and Structural Dynamics of Prion Proteins and Prions. Focus on Structural Biology, vol 9. Springer, Dordrecht. https://doi.org/10.1007/978-94-017-7318-8_3
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DOI: https://doi.org/10.1007/978-94-017-7318-8_3
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