title: Zinc modulates copper coordination mode in prion protein octa-repeat subdomains.
abstract: In this work we present and analyse XAS measurements carried out on various portions of Prion-protein tetra-octa-repeat peptides in complexes with Cu(II) ions, both in the presence and in the absence of Zn(II). Because of the ability of the XAS technique to provide detailed local structural information, we are able to demonstrate that Zn acts by directly interacting with the peptide, in this way competing with Cu for binding with histidine. This finding suggests that metal binding competition can be important in the more general context of metal homeostasis.
authors.affiliation: Dipartimento di Fisica, Università di Roma Tor Vergata, Via della Ricerca Scientifica, 1, 00133, Rome, Italy.
authors.forename: Francesco
authors.initials: F
authors.lastname: Stellato
authors.forename: Ann
authors.initials: A
authors.lastname: Spevacek
authors.forename: Olivier
authors.initials: O
authors.lastname: Proux
authors.forename: Velia
authors.initials: V
authors.lastname: Minicozzi
authors.forename: Glenn
authors.initials: G
authors.lastname: Millhauser
authors.forename: Silvia
authors.initials: S
authors.lastname: Morante
mesh_terms: D000595:Amino Acid Sequence; D003300:Copper / Q000378:metabolism*; D004578:Electron Spin Resonance Spectroscopy; D005583:Fourier Analysis; D010446:Peptide Fragments / Q000737:chemistry* / Q000378:metabolism*; D011328:Prions / Q000737:chemistry*; D017434:Protein Structure, Tertiary; D020449:Repetitive Sequences, Amino Acid; D056928:X-Ray Absorption Spectroscopy; D015032:Zinc / Q000378:metabolism*
chemical_list: D010446:Peptide Fragments; D011328:Prions; D003300:Copper; D015032:Zinc