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PMID:18942875

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Citation

Gaggelli, E, Jankowska, E, Kozlowski, H, Marcinkowska, A, Migliorini, C, Stanczak, P, Valensin, D and Valensin, G (2008) 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. J Phys Chem B 112:15140-50

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 Cu(2+) binding proteins, it appears relevant to compare the impact of Cu(2+) on the stability constants and structures of "physiological" complexes. After having comprehensively delineated the interaction of Cu(2+) with mammalian and avian PrPs, the stabilities and molecular structures of species generated by Cu(2+) 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 Cu(2+) 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.

Links

PubMed Online version:10.1021/jp804759q

Keywords

Amino Acid Sequence; Animals; Circular Dichroism; Copper/metabolism; Electron Spin Resonance Spectroscopy; Molecular Sequence Data; Nuclear Magnetic Resonance, Biomolecular; Prions/chemistry; Prions/metabolism; Spectrophotometry, Ultraviolet; Zebrafish

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

DANRE:A9C3N3

enables

GO:0005507: copper ion binding

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

DANRE:Q7T2P9

enables

GO:0005507: copper ion binding

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete


See also

References

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