Backbone resonance assignment of a proteolysis-resistant fragment in the oxygen-dependent degradation domain of the hypoxia inducible factor 1alpha.

Hypoxia-inducible factor 1alpha (HIF1alpha) 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 HIF1alpha responsible for the negative regulation of HIF1alpha in normoxia is intrinsically unfolded. Here, we carried out the backbone (1)H, (15)N, and (13)C resonance assignment of a proteolysis-resistant fragment (residues 404-477) in the HIF1alpha ODD domain using NMR spectroscopy. About 98% (344/352) of all the (1)HN, (15)N, (13)Calpha, (13)Cbeta, and (13)CO resonances were unambiguously assigned. The results will be useful for further investigation of the structural and dynamic states of the HIF1alpha ODD domain and its interaction with binding partners.