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

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journal contribution
posted on 08.05.2018, 08:51 by M. I. Abboud, T. E. McAllister, I. K. H. Leung, R. Chowdhury, C. Jorgensen, C. Domene, J. Mecinović, K. Lippl, R. L. Hancock, Richard J. Hopkinson, A. Kawamura, T. D. W. Claridge, C. J. Schofield
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.

History

Citation

Chemical Communications, 2018, 54 (25), pp. 3130-3133

Author affiliation

/Organisation/COLLEGE OF SCIENCE AND ENGINEERING/Department of Chemistry

Version

VoR (Version of Record)

Published in

Chemical Communications

Publisher

Royal Society of Chemistry

issn

1359-7345

eissn

1364-548X

Acceptance date

31/01/2018

Copyright date

2018

Available date

08/05/2018

Publisher version

http://pubs.rsc.org/en/Content/ArticleLanding/2018/CC/C8CC00387D#!divAbstract

Language

en