XAFS study of the high-affinity copper-binding site of human PrP 91–231 and its low-resolution structure in solution 1 1Edited by I. A. Wilson

• DOI: 10.1006/jmbi.2001.4795
• Publication Date: 2002-09-18T15:51:29Z
• Authors: S.Samar Hasnain; Loretta M. Murphy; Richard W. Strange; J.Günter Grossmann; Anthony R. Clarke; Graham S. Jackson; John Collinge
• Keywords: Envelope (radar)

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.