title: The structure function relationship for the Prion protein.
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.
authors.affiliation: Department of Industrial Microbiology, Ardmore House, University College Dublin, Belfield, Dublin 4, Ireland.
authors.forename: Marguerite E
authors.initials: ME
authors.lastname: Deignan
authors.forename: Marguerite
authors.initials: M
authors.lastname: Prior
authors.forename: Lorraine E
authors.initials: LE
authors.lastname: Stuart
authors.forename: Emma J
authors.initials: EJ
authors.lastname: Comerford
authors.forename: Hilary E M
authors.initials: HE
authors.lastname: McMahon
mesh_terms: D001692:Biological Transport / Q000502:physiology; D002352:Carrier Proteins / Q000378:metabolism; D003300:Copper / Q000378:metabolism; D006031:Glycosylation; D006360:Heat-Shock Proteins / Q000378:metabolism; D006801:Humans; D007797:Laminin / Q000378:metabolism; D017096:Prion Diseases / Q000378:metabolism* / Q000503:physiopathology; D011328:Prions / Q000378:metabolism*; D015398:Signal Transduction / Q000502:physiology
chemical_list: D002352:Carrier Proteins; D006360:Heat-Shock Proteins; D007797:Laminin; D011328:Prions; C429767:TP53INP1 protein, human; D003300:Copper