2-oxoglutarate regulates binding of hydroxylated hypoxia-inducible factor to prolyl hydroxylase domain 2

Prolyl hydroxylation of hypoxia inducible factor (HIF)-α, as catalysed by the Fe(II)/2-oxoglutarate (2OG)-dependent prolyl hydroxylase domain (PHD) enzymes, has a hypoxia sensing role in animals. We report that binding of prolyl-hydroxylated HIF-α to PHD2 is ~50 fold hindered by prior 2OG binding; t...

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Main Authors: Abboud, M, McAllister, T, Leung, I, Chowdhury, R, Jorgensen, C, Domene, C, Mecinović, J, Lippl,, K, Hancock, R, Hopkinson, R, Kawamura, A, Claridge, T, Schofield, C
Format: Journal article
Published: Royal Society of Chemistry 2018
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author Abboud, M
McAllister, T
Leung, I
Chowdhury, R
Jorgensen, C
Domene, C
Mecinović, J
Lippl,, K
Hancock, R
Hopkinson, R
Kawamura, A
Claridge, T
Schofield, C
author_facet Abboud, M
McAllister, T
Leung, I
Chowdhury, R
Jorgensen, C
Domene, C
Mecinović, J
Lippl,, K
Hancock, R
Hopkinson, R
Kawamura, A
Claridge, T
Schofield, C
author_sort Abboud, M
collection OXFORD
description Prolyl hydroxylation of hypoxia inducible factor (HIF)-α, as catalysed by the Fe(II)/2-oxoglutarate (2OG)-dependent prolyl hydroxylase domain (PHD) enzymes, has a hypoxia sensing role in animals. We report that binding of prolyl-hydroxylated HIF-α to PHD2 is ~50 fold hindered by prior 2OG binding; thus, when 2OG is limiting, HIF-α degradation might be inhibited by PHD binding
first_indexed 2024-03-06T21:00:38Z
format Journal article
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institution University of Oxford
last_indexed 2024-03-06T21:00:38Z
publishDate 2018
publisher Royal Society of Chemistry
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spelling oxford-uuid:3ac24af1-3ca0-4ba4-9c27-f26f64a0b7eb2022-03-26T14:03:32Z2-oxoglutarate regulates binding of hydroxylated hypoxia-inducible factor to prolyl hydroxylase domain 2Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:3ac24af1-3ca0-4ba4-9c27-f26f64a0b7ebSymplectic Elements at OxfordRoyal Society of Chemistry2018Abboud, MMcAllister, TLeung, IChowdhury, RJorgensen, CDomene, CMecinović, JLippl,, KHancock, RHopkinson, RKawamura, AClaridge, TSchofield, CProlyl hydroxylation of hypoxia inducible factor (HIF)-α, as catalysed by the Fe(II)/2-oxoglutarate (2OG)-dependent prolyl hydroxylase domain (PHD) enzymes, has a hypoxia sensing role in animals. We report that binding of prolyl-hydroxylated HIF-α to PHD2 is ~50 fold hindered by prior 2OG binding; thus, when 2OG is limiting, HIF-α degradation might be inhibited by PHD binding
spellingShingle Abboud, M
McAllister, T
Leung, I
Chowdhury, R
Jorgensen, C
Domene, C
Mecinović, J
Lippl,, K
Hancock, R
Hopkinson, R
Kawamura, A
Claridge, T
Schofield, C
2-oxoglutarate regulates binding of hydroxylated hypoxia-inducible factor to prolyl hydroxylase domain 2
title 2-oxoglutarate regulates binding of hydroxylated hypoxia-inducible factor to prolyl hydroxylase domain 2
title_full 2-oxoglutarate regulates binding of hydroxylated hypoxia-inducible factor to prolyl hydroxylase domain 2
title_fullStr 2-oxoglutarate regulates binding of hydroxylated hypoxia-inducible factor to prolyl hydroxylase domain 2
title_full_unstemmed 2-oxoglutarate regulates binding of hydroxylated hypoxia-inducible factor to prolyl hydroxylase domain 2
title_short 2-oxoglutarate regulates binding of hydroxylated hypoxia-inducible factor to prolyl hydroxylase domain 2
title_sort 2 oxoglutarate regulates binding of hydroxylated hypoxia inducible factor to prolyl hydroxylase domain 2
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