title: Backbone 1H, 13C, and 15N resonance assignments for the 26-kD human de-ubiquitinating enzyme UCH-L3.
abstract: 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.
authors.affiliation: Department of Biochemistry and Molecular Biology, University College London, Darwin Building, Gower Street, London WC1E6BT, UK.
authors.forename: Richard
authors.initials: R
authors.lastname: Harris
authors.forename: Ulf
authors.initials: U
authors.lastname: Eidhoff
authors.forename: Daniela
authors.initials: D
authors.lastname: Vinzenz
authors.forename: Martin
authors.initials: M
authors.lastname: Renatus
authors.forename: Bernd
authors.initials: B
authors.lastname: Gerhartz
authors.forename: Ulrich
authors.initials: U
authors.lastname: Hommel
authors.forename: Paul C
authors.initials: PC
authors.lastname: Driscoll
mesh_terms: 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
chemical_list: D011994:Recombinant Proteins; C509806:UCHL3 protein, human; D043222:Ubiquitin Thiolesterase; D003546:Cysteine Endopeptidases