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Home / Equine Research Bank / J Biomol Struct Dyn / The structural stability of wild-type horse prion protein.
Journal of biomolecular structure & dynamics2011; 29(2); 369-377; doi: 10.1080/07391102.2011.10507391

The structural stability of wild-type horse prion protein.

Abstract: Prion diseases (e.g. Creutzfeldt-Jakob disease (CJD), variant CJD (vCJD), Gerstmann-Straussler-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.
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Publication Date: 2011-08-31 PubMed ID: 21875155DOI: 10.1080/07391102.2011.10507391Google Scholar: Lookup
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  • Journal Article
  • Research Support
  • Non-U.S. Gov't

Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

This research article explores the structural stability of wild-type horse prion protein and its potential as a drug target for prion diseases.

Objective of the Study

  • The primary aim of this study was to understand the structural stability of the wild-type horse prion protein. This is particularly important as prion diseases are fatal and highly infectious neurodegenerative diseases with no known effective therapeutic approaches.
  • The research stems from the observation that horses, along with rabbits and dogs, are resistant to prion diseases. The goal was to explore the reasons behind this resistance and whether it could offer a potential solution to human infection.

Key Points from the Study

  • The researchers found that both rabbit and horse prion proteins possess a strong salt bridge ASP177-ARG163 that adds to their structural stability. This points to the possibility of this salt bridge being a potential drug target for prion diseases.
  • The study also uncovered four other salt bridges (GLU196-ARG156-HIS187, ARG156-ASP202, and GLU211-HIS177) that significantly contribute to the structural stability of horse prion protein.
  • A comprehensive database of salt bridges, hydrogen bonds, and hydrophobic contacts for horse prion protein was established during the course of this research.

Significance and Potential Application of the Study

  • If the β2-α2 loop and its associated salt bridges prove to be a successful drug target, this could progress the development of potential treatments for prion diseases.
  • The detailed database of salt bridges, hydrogen bonds, and hydrophobic contacts for horse prion protein can be used for further research and drug development. It offers valuable information for the understanding of prion-protein interactions.

Conclusion

  • The research provides valuable insights into why certain mammalian species, such as horses, are resistant to prion diseases. The structural stability provided by certain salt bridges appear key to this resistance.
  • This understanding brings the potential for developing therapeutic solutions for prion diseases. However, further research will be needed to validate these findings and develop effective treatment strategies.

Cite This Article

APA
Zhang J. (2011). The structural stability of wild-type horse prion protein. J Biomol Struct Dyn, 29(2), 369-377. https://doi.org/10.1080/07391102.2011.10507391

Publication

Journal of biomolecular structure & dynamics
ISSN: 1538-0254
NlmUniqueID: 8404176
Country: England
Language: English
Volume: 29
Issue: 2
Pages: 369-377

Researcher Affiliations

Zhang, Jiapu
  • School of Sciences, Information Technology and Engineering, University of Ballarat, Mount Helen, Ballarat, Victoria 3353, Australia. jiapu_zhang@hotmail.com

MeSH Terms

  • Amino Acid Sequence
  • Animals
  • Horses
  • Hydrogen Bonding
  • Models, Molecular
  • Molecular Sequence Data
  • Prions / chemistry
  • Protein Conformation
  • Protein Stability
  • Sequence Alignment

Citations

This article has been cited 18 times.
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