Fig. 1. Schematic structures of HIF1α and HIF1β domains. Both HIF1α and HIF1β possess bHLH and PAS domains for the formation of heterodimeric complexes and for DNA binding. HIF1α has two transactivation domains (NTAD and CTAD) and an inhibitory domain (ID), whereas HIF1β possesses only the CTAD domain. PHD hydroxylases possess two proline residues (P402 and P564) in the NTAD domain, whereas FIH hydroxylases possess an asparagine residue (N803) in the CTAD domain in HIF1α. These hydroxylated residues are ubiquitinated by VHL.
© 2019 International Journal of Stem Cells