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
  • Sophie E. Jackson
  • Shang-Te Danny Hsu
Article

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
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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.

Keywords

De-ubiquitinationUbiquitin C-terminal hydrolaseKnotted proteinsParkinson’s disease

Copyright information

© Springer Science+Business Media B.V. 2009

Authors and Affiliations

  • Fredrik I. Andersson
    • 1
  • Sophie E. Jackson
    • 1
  • Shang-Te Danny Hsu
    • 1
  1. 1.Department of ChemistryUniversity of CambridgeCambridgeUK