Structure of an HIF-1α-pVHL Complex: Hydroxyproline Recognition in Signaling

By Jung-Hyun Min, Haifeng Yang, M. Ivan, F. Gertler, W. Kaelin, N. Pavletich. Science, 2002

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Succinate links TCA cycle dysfunction to oncogenesis by inhibiting HIF-alpha prolyl hydroxylase. (2005, background): “HIF- subunit is the oxygen-inducible component of the orders of magnitude (Hon et al., 2002; Min et al., 2002).”
The General Transcription Machinery and General Cofactors (2006, background): “…normaxia), in which recognition of the hydroxylated proline (mediated by prolyl-4-hydroxylase) by the hydrophobic pocket located at the β-domain of pVHL (Hon et al., 2002; Min et al., 2002) eventually leads to the ubiquitination and degradation of HIF-1α (Jaakkola et al., 2001; Ivan et al., 2001).”
Ubiquitin: structures, functions, mechanisms. (2004, methodology): “This proposal was confirmed by structures of a hydroxylated HIF-1a peptide bound to VHL [130,131].”
Contrasting Properties of Hypoxia-Inducible Factor 1 (HIF-1) and HIF-2 in von Hippel-Lindau-Associated Renal Cell Carcinoma (2005, background): “Both proteins contain two conserved sites of prolyl hydroxylation that are independently targeted by a single hydroxyproline binding site within the domain of VHL (10, 30 ).”