Ubiquitin stability and the lys 63-linked polyubiquitination site are compromised on copper binding.
Articolo
Data di Pubblicazione:
2007
Abstract:
Appetite for copper: Ubiquitin is a hallmark
of toxic aggregates in neurodegenerative
disorders, where metal ions are
believed to play a crucial role. Copper(II)
ions have been found to bind to ubiquitin
at a specific site involving the N-terminal
nitrogen of Met1 and three oxygen donor
ligands in a tetragonal geometry. The
affinity of this site for copper(II) is comparable
to that of other amyloidogenic
proteins involved in neurodegenerative
disorders.
of toxic aggregates in neurodegenerative
disorders, where metal ions are
believed to play a crucial role. Copper(II)
ions have been found to bind to ubiquitin
at a specific site involving the N-terminal
nitrogen of Met1 and three oxygen donor
ligands in a tetragonal geometry. The
affinity of this site for copper(II) is comparable
to that of other amyloidogenic
proteins involved in neurodegenerative
disorders.
Tipologia CRIS:
01.01 Articolo in rivista
Keywords:
copper; neurodegenerative diseases; NMR spectroscopy; ubiquitin
Elenco autori:
Rizzarelli, Enrico; Tabbi', Giovanni; Grasso, Giulia; Magri', Antonio; Milardi, Danilo
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