The structure function relationship for the Prion protein.
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.
Deignan
Marguerite E
ME
Department of Industrial Microbiology, Ardmore House, University College Dublin, Belfield, Dublin 4, Ireland.
Prior
Marguerite
M
Stuart
Lorraine E
LE
Comerford
Emma J
EJ
McMahon
Hilary E M
HE
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
D002352:Carrier Proteins; D006360:Heat-Shock Proteins; D007797:Laminin; D011328:Prions; C429767:TP53INP1 protein, human; D003300:Copper