Open AccessBackbone and ILV side-chain NMR resonance assignments of the catalytic domain of human deubiquitinating enzyme USP7
Author(s) -
Gabrielle J. Valles,
Alexandra Pozhidaeva,
Dmitry M. Korzhnev
Publication year - 2022
Publication title -
biomolecular nmr assignments
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.359
H-Index - 16
eISSN - 1874-2718
pISSN - 1874-270X
DOI - 10.1007/s12104-022-10079-2
Subject(s) - deubiquitinating enzyme , ubiquitin , chemistry , enzyme , side chain , isoleucine , allosteric regulation , stereochemistry , protease , valine , biochemistry , microbiology and biotechnology , biophysics , leucine , biology , amino acid , gene , organic chemistry , polymer
Ubiquitin specific protease 7 (USP7) is a deubiquitinating enzyme, which removes ubiquitin tag from numerous protein substrates involved in diverse cellular processes such as cell cycle regulation, apoptosis and DNA damage response. USP7 affects stability, interaction network and cellular localization of its cellular and viral substrates by controlling their ubiquitination status. The large 41 kDa catalytic domain of USP7 harbors the active site of the enzyme. Here we present a nearly complete (93%) NMR resonance assignment of isoleucine, leucine and valine (ILV) side-chains of the USP7 catalytic domain along with a refined nearly complete (93%) assignment of its backbone resonances. The reported ILV methyl group assignment will facilitate further NMR investigations of structure, interactions and conformational dynamics of the USP7 enzyme.