Backbone and side chain 1H, 13C, and 15N assignments of the ubiquitin-like domain of human HOIL-1L, an essential component of linear ubiquitin chain assembly complex

Yoshinori Uekusa, Syunsuke Mimura, Hiroaki Sasakawa, Eiji Kurimoto, Eri Sakata, Serve Olivier, Hirokazu Yagi, Fuminori Tokunaga, Kazuhiro Iwai, Koichi Kato

Research output: Contribution to journalArticle

5 Citations (Scopus)


HOIL-1L and its binding partner, HOIL-1L interacting protein (HOIP), are essential components of linear ubiquitin (Ub) chain assembly complex (LUBAC), a 600-kDa enzyme complex catalyzing elongation of a tandemly connected Ub chain, which serve as a regulator of NF-κB activation. Specific interaction between the N-terminal Ub-like domain (UBL) of HOIL-1L and the Ub-associated domain (UBA) located at the central region of HOIP is shown to be involved in the formation of LUBAC. For better understanding of the mechanisms underlying the generation of the linear Ub chains by LUBAC, it is necessary to characterize the UBL-UBA interaction on the basis of structural data, which, however, is not available to date. Here we report backbone and side chain NMR assignments of the UBL of human HOIL-1L. By inspection of chemical shift index, it was predicted that HOIL-1L-UBL assumes a Ub fold followed by an α-helical segment, offering the basis for determination its 3D structure and interaction with HOIP-UBA in solution.

Original languageEnglish
Pages (from-to)177-180
Number of pages4
JournalBiomolecular NMR Assignments
Issue number2
Publication statusPublished - 2012 Jan 1



  • HOIL-1L
  • NMR spectroscopy
  • Resonance assignment
  • Ubiquitin-like domain

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry

Cite this