Studies on the structural stability of rabbit prion probed by molecular dynamics simulations of its wild-type and mutants.
Prion diseases are invariably fatal and highly infectious neurodegenerative diseases that affect humans and animals. Rabbits are the only mammalian species reported to be resistant to infection from prion diseases isolated from other species (Vorberg et al., 2003). Fortunately, the NMR structure of rabbit prion (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. This paper studies these NMR structures by molecular dynamics simulations. Simulation results confirm the structural stability of wild-type rabbit prion, and show that the salt bridge between D177 and R163 greatly contributes to the structural stability of rabbit prion protein.
Zhang
Jiapu
J
Victorian Life Sciences Computation Initiative, The University of Melbourne, 1 Hull Road, Croydon, VIC 3136, Australia. jiapu_zhang@hotmail.com
D019943:Amino Acid Substitution; D000818:Animals; D006860:Hydrogen Bonding; D006863:Hydrogen-Ion Concentration; D056004:Molecular Dynamics Simulation; D019906:Nuclear Magnetic Resonance, Biomolecular; D011328:Prions / Q000737:chemistry*; D011487:Protein Conformation; D055550:Protein Stability; D017433:Protein Structure, Secondary; D011817:Rabbits
D011328:Prions