Structural basis for binding of hypoxia-inducible factor to the oxygen-sensing prolyl hydroxylases.

Journal article

The oxygen-dependent hydroxylation of proline residues in the alpha subunit of hypoxia-inducible transcription factor (HIFalpha) is central to the hypoxic response in animals. Prolyl hydroxylation of HIFalpha increases its binding to the von Hippel-Lindau protein (pVHL), so signaling for degradation via the ubiquitin-proteasome system. The HIF prolyl hydroxylases (PHDs, prolyl hydroxylase domain enzymes) are related to the collagen prolyl hydroxylases, but form unusually stable complexes with...

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Authors: Chowdhury, R; McDonough, M; Mecinović, J; Loenarz, C; Flashman, E

• Publication status: Published
• Journal: Structure (London, England : 1993)
• Volume: 17
• Issue: 7
• Pages: 981-989
• Publication date: 2009-07-01
• DOI: 10.1016/j.str.2009.06.002
• EISSN: 1878-4186
• ISSN: 0969-2126
• Language: English
• Keywords: Signal Transduction; Humans; Crystallography, X-Ray; Models, Molecular; Hypoxia-Inducible Factor 1; Binding Sites; Hydroxylation; Proteasome Endopeptidase Complex; Protein Conformation; Anoxia; Von Hippel-Lindau Tumor Suppressor Protein; Protein Structure, Secondary; Proline; Catalytic Domain; Catalysis; Protein Structure, Tertiary; Ketoglutaric Acids; Hydroxyproline; Ubiquitin-Protein Ligases; Protein Binding; Oxygen; Procollagen-Proline Dioxygenase