XAFS study of the high-affinity copper-binding site of human PrP(91-231) and its low-resolution structure in solution

Autor:	S S, Hasnain, L M, Murphy, R W, Strange, J G, Grossmann, A R, Clarke, G S, Jackson, J, Collinge
Rok vydání:	2001
Předmět:	Models Molecular Binding Sites Prions Protein Conformation X-Rays Peptide Fragments Recombinant Proteins Solutions Humans Scattering Radiation Histidine Oxidation-Reduction Copper Sequence Deletion
Zdroj:	Journal of molecular biology. 311(3)
ISSN:	0022-2836
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::900439ddca2b13e90ca6d1141d502121 https://pubmed.ncbi.nlm.nih.gov/11493001 Zobrazit plný text záznamu Full Text from ScienceDirect