NR AXET
AU Millhauser,G.L.
TI Copper and the prion protein: methods, structures, function, and disease.
QU Annual Review of Physical Chemistry 2007; 58: 299-320
PT journal article; research support, n.i.h., extramural; research support, u.s. gov't, non-p.h.s.; review
AB The transmissible spongiform encephalopathies (TSEs) arise from conversion of the membrane-bound prion protein from PrPc to PrPsc. Examples of the TSEs include mad cow disease, chronic wasting disease in deer and elk, scrapie in goats and sheep, and kuru and Creutzfeldt-Jakob disease in humans. Although the precise function of PrPc in healthy tissues is not known, recent research demonstrates that it binds Cu(II) in an unusual and highly conserved region of the protein termed the octarepeat domain. This review describes recent connections between copper and PrPc, with an emphasis on the electron paramagnetic resonance elucidation of the specific copper-binding sites, insights into PrPc function, and emerging connections between copper and prion disease.
ZR 94
MH Animals; Copper/*chemistry/*metabolism; *Disease; Electron Spin Resonance Spectroscopy/methods; Humans; Prions/*chemistry/*metabolism; Protein Conformation
AD Department of Chemistry and Biochemistry, University of California, Santa Cruz, CA 95064, USA. glennm@chemistry.ucsc.edu
SP englisch
PO USA