Structure of Cu(I)-bound dj-1 reveals a biscysteinate metal binding site at the homodimer interface: Insights into mutational inactivation of dj-1 in parkinsonism

Journal of the American Chemical Society

Volumn 135, Issue 43, 2013, Pages 15974-15977

  Puno, M Rhyan ^a   Patel, Nisha A ^b   Møller, Simon Geir ^c,d   Robinson, Carol V ^b   Moody, Peter C E ^e   Odell, Mark ^a  

^a UNIVERSITY OF WESTMINSTER   (United Kingdom)

^b UNIVERSITY OF OXFORD   (United Kingdom)

^c STAVANGER UNIVERSITY HOSPITAL   (Norway)

^d ST JOHN'S UNIVERSITY   (United States)

^e UNIVERSITY OF LEICESTER   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE RESIDUES; DISSOCIATION CONSTANT; HOMODIMER INTERFACE; MASS SPECTROMETRIC ANALYSIS; METAL BINDING SITES; METAL COORDINATION; PARKINSONISM-LINKED MUTATIONS; SUPEROXIDE DISMUTASES;

AMINO ACIDS; COPPER; DISSOCIATION; METAL IONS; NEURODEGENERATIVE DISEASES; OXYGEN;

BINDING SITES;

COPPER ION; CYSTEINE; DJ 1 PROTEIN; HOMODIMER;

ARTICLE; BINDING SITE; CRYSTAL STRUCTURE; DISSOCIATION CONSTANT; METAL BINDING; MOLECULAR INTERACTION; PARKINSONISM; PROTEIN STRUCTURE; SPECTROSCOPY;

BINDING SITES; COPPER; CRYSTALLOGRAPHY, X-RAY; CYSTEINE; HUMANS; INTRACELLULAR SIGNALING PEPTIDES AND PROTEINS; MASS SPECTROMETRY; METALS; MODELS, MOLECULAR; MUTATION; ONCOGENE PROTEINS; PARKINSON DISEASE; PROTEIN CONFORMATION; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION; SUPEROXIDE DISMUTASE;

EID: 84887083797     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/ja406010m     Document Type: Article

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