title: Backbone assignments of the 26 kDa neuron-specific ubiquitin carboxyl-terminal hydrolase L1 (UCH-L1).
abstract: UCH-L1 is a member of the family of ubiquitin C-terminal hydrolases whose primary role is to hydrolyze small C-terminal adducts of ubiquitin to generate free ubiquitin monomers. Expression of UCH-L1 is highly specific to neurons and point mutations in this enzyme are associated with a hereditary form of Parkinson's disease. Herein, we present the NMR backbone assignments of human UCH-L1, thus enabling future solution-state NMR spectroscopic studies on the structure and function of this important protein.
authors.affiliation: Department of Chemistry, University of Cambridge, Lensfield Road, CB2 1EW Cambridge, UK.
authors.forename: Fredrik I
authors.initials: FI
authors.lastname: Andersson
authors.forename: Sophie E
authors.initials: SE
authors.lastname: Jackson
authors.forename: Shang-Te Danny
authors.initials: ST
authors.lastname: Hsu
mesh_terms: D003546:Cysteine Endopeptidases / Q000737:chemistry / Q000235:genetics; D004926:Escherichia coli; D006801:Humans; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000737:chemistry; D040681:Structural Homology, Protein; D043222:Ubiquitin Thiolesterase / Q000737:chemistry* / Q000235:genetics
chemical_list: D011994:Recombinant Proteins; C482860:UCHL1 protein, human; C509806:UCHL3 protein, human; D043222:Ubiquitin Thiolesterase; D003546:Cysteine Endopeptidases