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

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posted on 2018-05-08, 08:51 authored 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.

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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

2018-01-31

Copyright date

2018

Available date

2018-05-08

Publisher version

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

Language

en

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