Abstract：
:The prion protein (PrP) is a cell-surface Cu2+ binding glycoprotein which can bind six copper ions. The role of Cu2+ in PrP function, misfolding, and prion disease has generated much interest; however, the field has been hampered by a lack of consensus with regard to the affinity of Cu2+ for PrPC. Here we build on our understanding of the appearance of visible CD spectra for full-length PrP and fragments to determine the affinity of Cu2+ for four different binding modes, with dissociation constants ranging between 13 and 66 nM at pH 7.4.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Nadal RC,Davies P,Brown DR,Viles JHdoi
10.1021/bi9011397subject
Has Abstractpub_date
2009-09-29 00:00:00pages
8929-31issue
38eissn
0006-2960issn
1520-4995journal_volume
48pub_type
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