Complete 1H, 13C, 15N resonance assignments and secondary structure of the Vpr binding region of hHR23A (residues 223-363)

Biomol NMR Assign. 2020 Apr;14(1):13-17. doi: 10.1007/s12104-019-09913-x. Epub 2019 Aug 28.

Abstract

Comprehensive resonance assignments and delineation of the secondary structure elements of the C-terminal Vpr-binding region of hHR23A, residues 223-363, were achieved by triple-resonance NMR experiments on uniformly 13C,15N-labeled protein. Assignments are 100% and > 95% complete for backbone and side-chain resonances, respectively. This data constitutes important complementary information for our ongoing structure determination of the Vpr-hHR23A(223-363) complex. At high concentrations, severe line-broadening was observed for several residues in the 1H-15N HSQC spectrum, most likely resulting from inter-molecular interactions.

Keywords: DNA repair protein; RAD23; Vpr-binding; hHR23A.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Amino Acid Sequence
  • Carbon-13 Magnetic Resonance Spectroscopy*
  • DNA Repair Enzymes / chemistry*
  • DNA Repair Enzymes / metabolism*
  • DNA-Binding Proteins / chemistry*
  • DNA-Binding Proteins / metabolism*
  • Humans
  • Nitrogen Isotopes
  • Protein Binding
  • Protein Structure, Secondary
  • Proton Magnetic Resonance Spectroscopy*
  • vpr Gene Products, Human Immunodeficiency Virus / metabolism*

Substances

  • DNA-Binding Proteins
  • Nitrogen Isotopes
  • Nitrogen-15
  • vpr Gene Products, Human Immunodeficiency Virus
  • RAD23A protein, human
  • DNA Repair Enzymes