Backbone 1H, 13C, and 15N resonance assignments for the 26-kD human de-ubiquitinating enzyme UCH-L3.
To facilitate NMR spectroscopy studies of interactions with various ligands and potential inhibitors, we report the NMR backbone resonance assignments for the 26 kD human enzyme UCH-L3, a member of the ubiquitin C-hydrolase family of ubiquitin-specific cysteine proteases.
Harris
Richard
R
Department of Biochemistry and Molecular Biology, University College London, Darwin Building, Gower Street, London WC1E6BT, UK.
Eidhoff
Ulf
U
Vinzenz
Daniela
D
Renatus
Martin
M
Gerhartz
Bernd
B
Hommel
Ulrich
U
Driscoll
Paul C
PC
D020134:Catalytic Domain; D003546:Cysteine Endopeptidases / Q000737:chemistry* / Q000235:genetics; D006801:Humans; D015394:Molecular Structure; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D043222:Ubiquitin Thiolesterase
D011994:Recombinant Proteins; C509806:UCHL3 protein, human; D043222:Ubiquitin Thiolesterase; D003546:Cysteine Endopeptidases