Backbone 1H, 15N, and 13C resonance assignments and secondary structure of the Tollip CUE domain

Hugo F. Azurmendi, Sharmistha Mitra, Iriscilla Ayala, Liwu Li, Carla V. Finkielstein, Daniel G.S. Capelluto

Research output: Contribution to journalArticlepeer-review

10 Scopus citations


The Toll-interacting protein (Tollip) is a negative regulator of the Toll-like receptor (TLR)-mediated inflammation response. Tollip is a modular protein that contains an N-terminal Tom1-binding domain (TBD), a central conserved domain 2 (C2), and a C-terminal coupling of ubiquitin to endoplasmic reticulum degradation (CUE) domain. Here, we report the sequence-specific backbone 1H, 15N, and 13C assignments of the human Tollip CUE domain. The CUE domain was found to be a stable dimer as determined by size-exclusion chromatography and molecular crosslinking studies. Analysis of the backbone chemical shift data indicated that the CUE domain exhibits three helical elements corresponding to 52% of the protein backbone. Circular dichroism spectrum analysis confirmed the helical nature of this domain. Comparison of the location of these helical regions with those reported for yeast CUE domains suggest differences in length for all helical elements. We expect the structural analysis presented here will be the foundation for future studies on the biological significance of the Tollip CUE domain, its molecular interactions, and the mechanisms that modulate its function during the inflammatory response.

Original languageEnglish (US)
Pages (from-to)581-585
Number of pages5
JournalMolecules and Cells
Issue number6
StatePublished - Dec 2010
Externally publishedYes


  • CUE domain
  • Innate immunity
  • NMR spectroscopy
  • Resonance assignments
  • Toll-like receptor
  • Tollip

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology


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