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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.
Autorzy
Rok wydania
2008
Czasopismo
Journal of Physical Chemistry B
Numer woluminu
112
Strony
15140-15150
DOI
10.1021/jp804759q
Kolekcja
Język
Angielski
Typ publikacji
Artykuł
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.
Adres publiczny
https://doi.org/10.1021/jp804759q
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