Backbone assignments of the 26 kDa neuron-specific ubiquitin carboxyl-terminal hydrolase L1 (UCH-L1).
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.
Andersson
Fredrik I
FI
Department of Chemistry, University of Cambridge, Lensfield Road, CB2 1EW Cambridge, UK.
Jackson
Sophie E
SE
Hsu
Shang-Te Danny
ST
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
D011994:Recombinant Proteins; C482860:UCHL1 protein, human; C509806:UCHL3 protein, human; D043222:Ubiquitin Thiolesterase; D003546:Cysteine Endopeptidases