Abstract / Description of output
Deimination is the post-translational conversion of arginine residues to citrulline. It has been implicated as a causative factor in autoimmune diseases such as multiple sclerosis and rheumatoid arthritis and more recently, as a marker of neurodegeneration. We have investigated the effect of the post-translational modification of arginine residues on the structure of recombinant ovine prion protein. Deiminated prion protein exhibited biophysical properties characteristic of the scrapie-associated conformer of prion protein viz. an increased β-sheet secondary structure, congophilic structures indicative of amyloid and proteinase K resistance which could be templated onto normal unmodified prion protein. In the light of these findings, a potential role of post-translational modifications to prion protein in disease initiation or propagation is discussed.
Original language | English |
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Pages (from-to) | 1123-1133 |
Journal | BBA - Proteins and Proteomics |
Volume | 1794 |
Publication status | Published - 2009 |
Keywords / Materials (for Non-textual outputs)
- Prion protein
- Post-translational modification
- conformational change
- Deimination
- Citrulline
- Arginine modificaiton
- Amyloid