Studies on the structural stability of rabbit prion probed by molecular dynamics simulations.
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 (I. Vorberg et al., Journal of Virology 77 (3), 2003-2009 (2003)). At the end of 2007 the NMR structure of rabbit prion (124-228) was deposited into protein data bank (PDB entry 2FJ3). This paper studies the inhibition mechanism of rabbit prion at molecular structural level by molecular dynamics simulations.
Zhang
Jiapu
J
Centre for Informatics and Applied Optimization, School of ITMS, The University of Ballarat, 15/172 Princes St, Carlton North VIC 3054, Australia. jiapu_zhang@hotmail.com
D000595:Amino Acid Sequence; D000818:Animals; D006801:Humans; D056004:Molecular Dynamics Simulation; D008969:Molecular Sequence Data; D017096:Prion Diseases / Q000378:metabolism; D011328:Prions / Q000737:chemistry* / Q000235:genetics; D011487:Protein Conformation; D017510:Protein Folding; D011817:Rabbits
D011328:Prions