Abstract
Rabbits are highly resistant to naturally acquired prion diseases and even under experimental conditions induction of clinical disease is not easy. In this Chapter, we do 30 ns’ MD analyses of the following structures of rabbit prion protein (rabbitPrPC) and its mutants: Sect. 2.1 wild-type NMR structure (PDB entry 2FJ3), Sect. 2.2 wild-type X-ray structure (PDB entry 3O79), Sect. 2.3 I214V mutant (NMR PDB entry 2JOM), Sect. 2.4 S173N mutant (NMR PDB entry 2JOH, X-ray PDB entry 4HMM), Sect. 2.5 S170N mutant (X-ray PDB entry 4HLS), Sect. 2.6 S170N & S174N mutants (X-ray PDB entry 4HMR), and Sect. 2.7 the homology structure without the disulfide bond. We did MD at 300, 350, 450 K under neutral and low pH environments for Sects. 2.1–2.6, and for Sect. 2.7 at 300 K under neutral pH environment. MD analysis results confirmed the structural stability of wild-type rabbitPrPC and proposed some reasons to contribute to the structural stability of wild-type rabbitPrPC.
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Zhang, J. (2018). Rabbits: Wild-Type and Mutants. In: Molecular Dynamics Analyses of Prion Protein Structures. Focus on Structural Biology, vol 10. Springer, Singapore. https://doi.org/10.1007/978-981-10-8815-5_2
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DOI: https://doi.org/10.1007/978-981-10-8815-5_2
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