Unique structural properties associated with mouse prion Δ105-125 protein

[thumbnail of Open Access]
Preview
Text (Open Access) - Published Version
· Available under License Creative Commons Attribution.
· Please see our End User Agreement before downloading.
| Preview
Available under license: Creative Commons Attribution

Please see our End User Agreement.

It is advisable to refer to the publisher's version if you intend to cite from this work. See Guidance on citing.

Add to AnyAdd to TwitterAdd to FacebookAdd to LinkedinAdd to PinterestAdd to Email

Patel, A., Vasiljevic, S. and Jones, I. M. orcid id iconORCID: https://orcid.org/0000-0002-7738-2516 (2013) Unique structural properties associated with mouse prion Δ105-125 protein. PRION, 7 (3). pp. 235-243. ISSN 1933-690X 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

Altmetric Badge

Item Type Article
URI https://reading-clone.eprints-hosting.org/id/eprint/35064
Identification Number/DOI 10.4161/pri.24429
Refereed Yes
Divisions Life Sciences > School of Biological Sciences > Biomedical Sciences
Publisher Landes Bioscience
Download/View statistics View download statistics for this item

Downloads

Downloads per month over past year

University Staff: Request a correction | Centaur Editors: Update this record

Search Google Scholar