Molecular dynamics studies on the NMR and X-ray structures of rabbit prion proteins

DOI10.1016/J.JTBI.2013.10.005MaRDI QIDQ2632420zbMATH OpenOpenAlexWikidataFDO

Authors Jiapu Zhang, Yuanli Zhang

Publication date 14 May 2019

Published in Journal of Theoretical Biology (Search for Journal in Brave)

Full work available at URL https://arxiv.org/abs/1304.7633

zbMATH Keywords

molecular dynamics studyNMR and X-ray structuresprion diseasesrabbit prion proteinswild-type and mutants

Mathematics Subject Classification ID

Protein sequences, DNA sequences (92D20)

Abstract: Prion diseases are invariably fatal and highly infectious neurodegenerative diseases that affect a wide variety of mammalian species such as sheep, goats, mice, humans, chimpanzees, hamsters, cattle, elks, deer, minks, cats, chicken, pigs, turtles, etc. These neurodegenerative diseases are caused by the conversion from a soluble normal cellular protein into insoluble abnormally folded infectious prions and the conversion is believed to involve conformational change from a predominantly alpha-helical protein to one rich in beta-sheet structure. Such conformational changes may be amenable to study by molecular dynamics (MD) techniques. For rabbits, classical studies show they have a low susceptibility to be infected, but in 2012 it was reported that rabbit prion can be generated (though not directly) and the rabbit prion is infectious and transmissible (Proceedings of the National Academy of Sciences USA 109(13): 5080-5). This paper studies the NMR and X-ray molecular structures of rabbit prion protein wild-type and mutants by MD techniques, in order to understand the specific mechanism of rabbit prion protein and rabbit prions.

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Cites work

• Studies on the structural stability of rabbit prion probed by molecular dynamics simulations of its wild-type and mutants
• The disposition of the LZCC protein residues in wenxiang diagram provides new insights into the protein-protein interaction mechanism

Cited in

(5)

• Studies on the structural stability of rabbit prion probed by molecular dynamics simulations of its wild-type and mutants
• Control of the pathogenic conformational change of the prion protein by an attractor of low order
• The mechanism of pulsed electric field (PEF) targeting location on the spatial conformation of pine nut peptide
• Frameshifted prion proteins as pathological agents: quantitative considerations
• Spontaneous formation of annular structures observed in molecular dynamics simulations of polyglutamine peptides

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Uses Software

• Wenxiang

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