NMR Characterization of Oxidized Form of Human 8-kDa Dynein Light Chain
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Redox-dependent conformational change of human 8-kDa Dynein light chain (LC8) plays important role in regulating NF-κB signaling pathway. In this study we characterized the structural states of the oxidized and reduced forms of LC8 by using NMR spectroscopy. The 1H-15N 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.
Abstract
Redox-dependent conformational change of human 8-kDa Dynein light chain (LC8) plays important role in regulating NF-κB signaling pathway. In this study we characterized the structural states of the oxidized and reduced forms of LC8 by using NMR spectroscopy. The 1H-15N 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.
참고문헌 (8)
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