XAFS study of the high-affinity copper-binding site of human PrP(91-231) and its low-resolution structure in solution.
J Mol Biol
; 311(3): 467-73, 2001 Aug 17.
Article
em En
| MEDLINE
| ID: mdl-11493001
ABSTRACT
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.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Fragmentos de Peptídeos
/
Príons
/
Cobre
Limite:
Humans
Idioma:
En
Ano de publicação:
2001
Tipo de documento:
Article