(1)H, (13)C and (15)N backbone resonance assignment for the 40.5 kDa catalytic domain of Ubiquitin Specific Protease 7 (USP7)

Biomol NMR Assign. 2016 Oct;10(2):345-9. doi: 10.1007/s12104-016-9698-3. Epub 2016 Jul 8.

Abstract

The deubiquitinase Ubiquitin Specific Protease 7 (USP7) is part of the regulatory cascade of proteins that modulates the activity of the tumor suppressor protein p53. Deubiquitination of its target Murine Double Minute 2 (MDM2) leads to increased proteosomal degradation of p53. Consequently, USP7 has emerged as an attractive oncology target because its inhibition stabilizes p53, thereby promoting p53-dependent apoptosis in cancer cells. Here we report the backbone resonance assignment for the 40.5 kDa catalytic domain of USP7.

Keywords: Deubiquitinases; HAUSP; MDM2; NMR assignment; NMR spectroscopy; USP7; p53.

MeSH terms

  • Amino Acid Sequence
  • Catalytic Domain*
  • Humans
  • Nuclear Magnetic Resonance, Biomolecular*
  • Ubiquitin Thiolesterase / chemistry*
  • Ubiquitin Thiolesterase / metabolism
  • Ubiquitin-Specific Peptidase 7

Substances

  • USP7 protein, human
  • Ubiquitin Thiolesterase
  • Ubiquitin-Specific Peptidase 7