Q16665

HIF-1α also known as HIF1, MOP1, PASD8, HIF-1alpha is characterized by its multi-domain structure, including the basic helix-loop-helix (bHLH) domain essential for DNA binding, the PAS (Per-Arnt-Sim) domains that facilitate dimerization with HIF-1β (Arnt1), and the oxygen-dependent degradation (ODD) domain that regulates stability under normoxic conditions. HIF-1α contains transactivation domains crucial for recruiting co-activators and initiating transcription of target genes. Understanding the intricate structure of HIF-1α is critical, as this determines the ability to form the active HIF-1 complex, bind to hypoxia-responsive elements (HRE) in the genome, and activate transcription of genes involved in essential processes such as glycolysis, erythropoiesis, and angiogenesis, which are vital for restoring oxygen homeostasis and maintaining cell viability under hypoxic stress.