- Title
- The structural stability of wild-type horse prion protein
- Creator
- Zhang, Jiapu
- Date
- 2011
- Type
- Text; Journal article
- Identifier
- http://researchonline.federation.edu.au/vital/access/HandleResolver/1959.17/64428
- Identifier
- vital:4258
- Identifier
- ISSN:0739-1102
- Abstract
- Prion diseases (e.g. Creutzfeldt-Jakob disease (CJD), variant CJD (vCJD), Gerstmann-Sträussler-Scheinker syndrome (GSS), Fatal Familial Insomnia (FFI) and Kuru in humans, scrapie in sheep, bovine spongiform encephalopathy (BSE or 'mad-cow' disease) and chronic wasting disease (CWD) in cattles) are invariably fatal and highly infectious neurodegenerative diseases affecting humans and animals. However, by now there have not been some effective therapeutic approaches or medications to treat all these prion diseases. Rabbits, dogs, and horses are the only mammalian species reported to be resistant to infection from prion diseases isolated from other species. Recently, the β2-α2 loop has been reported to contribute to their protein structural stabilities. The author has found that rabbit prion protein has a strong salt bridge ASP177-ARG163 (like a taut bow string) keeping this loop linked. This paper confirms that this salt bridge also contributes to the structural stability of horse prion protein. Thus, the region of β2-α2 loop might be a potential drug target region. Besides this very important salt bridge, other four important salt bridges GLU196-ARG156-HIS187, ARG156-ASP202 and GLU211-HIS177 are also found to greatly contribute to the structural stability of horse prion protein. Rich databases of salt bridges, hydrogen bonds and hydrophobic contacts for horse prion protein can be found in this paper. ©Adenine Press (2011).
- Relation
- Journal of Biomolecular Structure and Dynamics Vol. 29, no. 2 (2011), p. 369-377
- Rights
- This metadata is freely available under a CCO license
- Subject
- Horse; Immunity; Molecular dynamics; Prion diseases; Arginine; Aspartic acid; Glutamic acid; Histidine; Prion protein; Dog; Hydrogen bond; Hydrophobicity; pH measurement; Protein stability; Protein structure; Rabbit; Sequence alignment; Species comparison; Structure analysis
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