The chemistry of copper binding to PrP: is there sufficient evidence to elucidate a role for copper in protein function?
There has been an enormous body of literature published in the last 10 years concerning copper and PrP (prion protein). Despite this, there is still no generally accepted role for copper in the function of PrP or any real consensus as to how and to what affinity copper associates with the protein. The present review attempts to look at all the evidence for the chemistry, co-ordination and affinity of copper binding to PrP, and then looks at what effect this has on the protein. We then connect this evidence with possible roles for PrP when bound to copper. No clear conclusions can be made from the available data, but it is clear from the present review what aspects of copper association with PrP need to be re-investigated.
Davies
Paul
P
Department of Biology and Biochemistry, University of Bath, Claverton Down, Bath BA2 7AY, U.K.
Brown
David R
DR
D000818:Animals; D000975:Antioxidants / Q000737:chemistry / Q000378:metabolism; D001665:Binding Sites; D003300:Copper / Q000737:chemistry / Q000378:metabolism*; D007700:Kinetics; D051379:Mice; D008958:Models, Molecular; D010446:Peptide Fragments / Q000737:chemistry; D011328:Prions / Q000737:chemistry* / Q000502:physiology*; D011487:Protein Conformation; D017510:Protein Folding
D000975:Antioxidants; D010446:Peptide Fragments; D011328:Prions; D003300:Copper