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Ubiquitin Stability and the Lys 63‐Linked Polyubiquitination Site Are Compromised on Copper Binding
Author(s) -
Milardi Danilo,
Arnesano Fabio,
Grasso Giulia,
Magrì Antonio,
Tabbì Giovanni,
Scintilla Simone,
Natile Giovanni,
Rizzarelli Enrico
Publication year - 2007
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200701987
Subject(s) - ubiquitin , copper , chemistry , binding site , tetragonal crystal system , biochemistry , crystallography , crystal structure , organic chemistry , gene
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 Met 1 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.