NR AFFD
AU Hasnain,S.S.; Murphy,L.M.; Strange,R.W.; Grossmann,J.G.; Clarke,A.R.; Jackson,G.S.; Collinge,J.
TI XAFS study of the high-affinity copper-binding site of human PrP(91-231) and its low-resolution structure in solution
QU Journal of Molecular Biology 2001 Aug 17; 311(3): 467-73
PT journal article
AB Here, we describe the structure of a C-terminal high-affinity copper-binding site within a truncated recombinant human PrP containing residues 91-231, which lacks the octapeptide repeat region. We show that at least two extra co-ordinating groups are involved in binding this copper(II) ion in conjunction with histidine residues 96 and 111 in a region of the molecule known to be critical in conferring strain type. In addition, using X-ray solution scattering, a low-resolution shape of PrP(91-231) is provided. The restored molecular envelope is consistent with the picture where the N-terminal segment, residues 91-120, extends out from the previously known globular domain containing residues 121-231.
MH Binding Sites; Copper/*metabolism; Histidine/genetics/metabolism; Human; Models, Molecular; Oxidation-Reduction; Peptide Fragments/*chemistry/genetics/isolation & purification/*metabolism; Prions/*chemistry/genetics/isolation & purification/*metabolism; Protein Conformation; Recombinant Proteins/chemistry/genetics/isolation &; purification/metabolism; Scattering, Radiation; Sequence Deletion/genetics; Solutions; Support, Non-U.S. Gov't; X-Rays
AD CCLRC Daresbury Laboratory, Daresbury, Warrington, Cheshire, UK
SP englisch
PO England