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NMR Characterization of Oxidized Form of Human 8-kDa Dynein Light Chain

  • Shin, Jae-Sun (Medical Proteomics Research Center, KRIBB) ;
  • Jeong, Woo-Jin (Department of Life Science, Division of Life and Pharmaceutical Sciences, Ewha Womans University) ;
  • Chi, Seung-Wook (Medical Proteomics Research Center, KRIBB)
  • Received : 2010.10.30
  • Accepted : 2010.12.09
  • Published : 2010.12.20

Abstract

Redox-dependent conformational change of human 8-kDa Dynein light chain (LC8) plays important role in regulating NF-${\kappa}B$ signaling pathway. In this study we characterized the structural states of the oxidized and reduced forms of LC8 by using NMR spectroscopy. The $^1H-^{15}N$ 2D HSQC spectra of oxidized LC8 indicated that no significant change in tertiary structure of LC8 occurred upon oxidation. The chemical shift perturbations of LC8 upon oxidation suggest a redox-dependent quaternary structural change.

Keywords

References

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