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http://dx.doi.org/10.1007/s10059-009-0065-4

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)
Publication Information
Molecules and Cells / v.27, no.4, 2009 , pp. 493-496 More about this Journal
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
hypoxia-inducible factor $1{\alpha}$; NMR spectroscopy; oxygen-dependent degradation domain; resonance assignment;
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