Biomolecular NMR Assignments

, Volume 4, Issue 1, pp 41–43

Backbone assignments of the 26 kDa neuron-specific ubiquitin carboxyl-terminal hydrolase L1 (UCH-L1)


  • Fredrik I. Andersson
    • Department of ChemistryUniversity of Cambridge
  • Sophie E. Jackson
    • Department of ChemistryUniversity of Cambridge
    • Department of ChemistryUniversity of Cambridge

DOI: 10.1007/s12104-009-9203-3

Cite this article as:
Andersson, F.I., Jackson, S.E. & Hsu, S.D. Biomol NMR Assign (2010) 4: 41. doi:10.1007/s12104-009-9203-3


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.


De-ubiquitinationUbiquitin C-terminal hydrolaseKnotted proteinsParkinson’s disease

Copyright information

© Springer Science+Business Media B.V. 2009