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

The backbone H, C and N 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 H- N signal intensities were boosted by an amide hydrogen exchange protocol, where...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Biomolecular NMR assignments 2024-06, Vol.18 (1), p.33
Hauptverfasser: Pandya, Maya J, Augustyniak, Wojciech, Cliff, Matthew J, Lindner, Ilka, Stinn, Anne, Kahmann, Jan, Temmerman, Koen, Dannatt, Hugh R W, Waltho, Jonathan P, Watson, Martin J
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
Beschreibung
Zusammenfassung:The backbone H, C and N 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 H- N signal intensities were boosted by an amide hydrogen exchange protocol, where expressed H, C, N-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.
ISSN:1874-270X