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

Abstract:
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
Publication status:
Published
Peer review status:
Peer reviewed
Version:
Publisher's version

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Publisher copy:
10.1039/C8CC00387D

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Institution:
University of Oxford
Division:
MPLS Division
Department:
Chemistry; Organic Chemistry
ORCID:
0000-0003-2141-5988
More by this author
Institution:
University of Oxford
Division:
MPLS Division
Department:
Chemistry; Organic Chemistry
Leung, IKH More by this author
More by this author
Institution:
University of Oxford
Division:
MPLS Division
Department:
Chemistry; Organic Chemistry
Jorgensen, C More by this author
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Wellcome Trust More from this funder
Cancer Research UK More from this funder
British Heart Foundation More from this funder
Publisher:
Royal Society of Chemistry Publisher's website
Journal:
Chemical Communications Journal website
Volume:
54
Issue:
25
Pages:
3130-3133
Publication date:
2018-03-09
Acceptance date:
2018-01-31
DOI:
EISSN:
1364-548X
ISSN:
1359-7345
Pubs id:
pubs:821941
URN:
uri:3ac24af1-3ca0-4ba4-9c27-f26f64a0b7eb
UUID:
uuid:3ac24af1-3ca0-4ba4-9c27-f26f64a0b7eb
Local pid:
pubs:821941

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