Molecules and Cells

Korean Society for Molecular and Cellular Biology (한국분자세포생물학회)
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Backbone Resonance Assignment of a Proteolysis-Resistant Fragment in the Oxygen-Dependent Degradation Domain of the Hypoxia Inducible Factor 1α

  • Kim, Do-Hyoung (Molecular Cancer Research Center, Korea Research Institute of Bioscience and Biotechnology) ;
  • Lee, Si-Hyung (Molecular Cancer Research Center, Korea Research Institute of Bioscience and Biotechnology) ;
  • Chi, Seung-Wook (Molecular Cancer Research Center, Korea Research Institute of Bioscience and Biotechnology) ;
  • Nam, Ki Hoon (Molecular Cancer Research Center, Korea Research Institute of Bioscience and Biotechnology) ;
  • Han, Kyou-Hoon (Molecular Cancer Research Center, Korea Research Institute of Bioscience and Biotechnology)
  • Received : 2008.12.01
  • Accepted : 2009.02.26
  • Published : 2009.04.30
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Abstract

Hypoxia-inducible factor $1{\alpha}$ ($HIF1{\alpha}$) is a transcription factor that plays a key role in the adaptation of cells to low oxygen stress and oxygen homeostasis. The oxygen-dependent degradation (ODD) domain of $HIF1{\alpha}$ responsible for the negative regulation of $HIF1{\alpha}$ in normoxia is intrinsically unfolded. Here, we carried out the backbone $^1H$, $^{15}N$, and $^{13}C$ resonance assignment of a proteolysis-resistant fragment (residues 404-477) in the $HIF1{\alpha}$ ODD domain using NMR spectroscopy. About 98% (344/352) of all the $^1HN$, $^{15}N$, $^{13}C{\alpha}$, $^{13}C{\beta}$, and $^{13}CO$ resonances were unambiguously assigned. The results will be useful for further investigation of the structural and dynamic states of the $HIF1{\alpha}$ ODD domain and its interaction with binding partners.

Keywords

Acknowledgement

Supported by : Korea Research Foundation, Korean Ministry of Science and Technology

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