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Unique structural properties associated with mouse prion Δ105-125 protein

Patel, A., Vasiljevic, S. and Jones, I. M. (2013) Unique structural properties associated with mouse prion Δ105-125 protein. PRION, 7 (3). pp. 235-243. ISSN 1933-690X

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To link to this item DOI: 10.4161/pri.24429

Abstract/Summary

Murine prion protein deleted for residues 105-125 is intrinsically neurotoxic and mediates a TSE-like phenotype in transgenic mice. Equivalent and overlapping deletions were expressed in E.coli, purified and analyzed. Among mutants spanning the region 95-135, a construct lacking solely residues 105-125 had distinct properties when compared with the full-length prion protein 23-231 or other deletions. This distinction was also apparent followed expression in eukaryotic cells. Unlike the full-length protein, all deletion mutants failed to bind to synthetic membranes in vitro. These data suggest a novel structure for the 105-125 deleted variant that may relate to its biological properties

Item Type:Article
Refereed:Yes
Divisions:Faculty of Life Sciences > School of Biological Sciences > Biomedical Sciences
ID Code:35064
Publisher:Landes Bioscience

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