Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/5513
Title: Structural characterization of the intra- and inter-repeat copper binding modes within the N-terminal region of "Prion Related Protein" (PrP-rel-2) of Zebrafish.
Authors: Gaggelli, Elena 
Jankowska, E
Kozlowski, H
Marcinkowska, A
Migliorini, Caterina
Stanczak, P
Valensin, Daniela 
Valensin, Gianni 
Issue Date: 2008
Project: None 
Journal: JOURNAL OF PHYSICAL CHEMISTRY. B, CONDENSED MATTER, MATERIALS, SURFACES, INTERFACES & BIOPHYSICAL
Abstract: 
The unique biology of prion proteins (PrPs) allied with the public-health risks posed by prion zoonoses, such as various animal neurodegenerations, has focused much attention on the molecular basis of the controls cross-species and on the similarities between PrPs from different species. Given the common feature of PrPs as Cu2+ binding proteins, it appears relevant to compare the impact of Cu2+ on the stability constants and structures of “physiological” complexes. After having comprehensively delineated the interaction of Cu2+ with mammalian and avian PrPs, the stabilities and molecular structures of species generated by Cu2+ interacting with the irregular repeated domain derived from Danio rerio zebrafish PrP-rel-2 were investigated. Copper complexes with different zebrafish PrP-rel-2 fragments were analyzed by potentiometric and spectroscopic techniques. The data were interpreted as to provide evidence of all investigated repeat units selectively binding Cu2+ via the His imidazole(s). The structural models obtained from paramagnetic NMR showed an intra- or inter-copper binding according to the number of the His in the sequence. In comparison to the mammalian and avian cases, the enzymatic function referred to SOD-like activity was shown to be rather faint in the fish PrPs cases.
Description: 
38116
URI: http://hdl.handle.net/20.500.12779/5513
ISSN: 1520-6106
DOI: 10.1021/jp804759q
Appears in Collections:Publications

Show full item record

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.