Backbone 1H, 13C and 15N resonance assignment of the ubiquitin specific protease 7 catalytic domain (residues 208–554) in complex with a small molecule ligand

MJ Pandya, W Augustyniak, MJ Cliff, I Lindner, A Stinn, J Kahmann, K Temmerman, HRW Dannatt, JP Waltho, MJ Watson

Research output: Contribution to journalArticlepeer-review

Abstract

The backbone 1H, 13C and 15N resonance assignment of Ubiquitin Specific Protease 7 catalytic domain (residues 208–554) was performed in its complex with a small molecule ligand and in its apo form as a reference. The amide 1H- 15N signal intensities were boosted by an amide hydrogen exchange protocol, where expressed 2H, 13C, 15N-labeled protein was unfolded and re-folded to ensure exchange of amide deuterons to protons. The resonance assignments were used to determine chemical shift perturbations on ligand binding, which are consistent with the binding site observed by crystallography.

Original languageEnglish
Pages (from-to)33-44
Number of pages12
JournalBiomolecular NMR Assignments
Volume18
Issue number1
Early online date12 Mar 2024
DOIs
Publication statusPublished - Jun 2024

Keywords

  • Amide hydrogen exchange
  • Chemical shift perturbation
  • Ligand binding
  • NMR resonance assignment
  • USP7

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