The structure function relationship for the Prion protein

Article type: Research Article

Authors: Deignan, Marguerite E. | Prior, Marguerite | Stuart, Lorraine E. | Comerford, Emma J. | McMahon, Hilary E.M.^{; *}

Affiliations: Department of Industrial Microbiology, Ardmore House, University College Dublin, Belfield, Dublin 4, Ireland

Correspondence: [*] Corresponding author: Hilary E.M. McMahon, Department of Industrial Microbiology, Ardmore House, University College Dublin, Belfield, Dublin 4, Ireland. Tel.: +353 1 7162828; Fax: +353 1 7161183; E-mail: hillary.mcmahon@ucd.ie.

Abstract: Central to Prion diseases is the normal endogenous Prion protein, PrPC. In spite of years of research the exact function of this protein remains enigmatic. Numerous binding partners have been identified for PrPC and due to the presence of a repeated sequence of PHGGGWGQ in the proteins amino-terminus it can bind metal ions. The protein is a complex molecule and each portion of PrPC possesses different roles for function and/ or trafficking. As understanding the role of PrPC is central to these disorders the structure/function relationship will be reviewed here.

Keywords: prion, carboxyl-terminus, amino-terminus, copper, glycosylation

DOI: 10.3233/JAD-2004-6309

Journal: Journal of Alzheimer's Disease, vol. 6, no. 3, pp. 283-289, 2004