期刊
FEBS JOURNAL
卷 278, 期 7, 页码 1086-1097出版社
WILEY-BLACKWELL
DOI: 10.1111/j.1742-4658.2011.08022.x
关键词
2-oxoglutarate-dependent dioxygenase; ankyrin repeat domain; factor inhibiting HIF; histidinyl hydroxylation; post-translational hydroxylation
资金
- Biotechnology and Biological Sciences Research Council
- European Union
- Wellcome Trust
Factor-inhibiting hypoxia-inducible factor (FIH) is an Fe(II)/2-oxogluta-rate-dependent dioxygenase that acts as a negative regulator of the hypoxia-inducible factor (HIF) by catalysing beta-hydroxylation of an asparaginyl residue in its C-terminal transcriptional activation domain (CAD). In addition to the hypoxia-inducible factor C-terminal transcriptional activation domain (HIF-CAD). FIH also catalyses asparaginyl hydroxylation of many ankyrin repeat domain-containing proteins, revealing a broad sequence selectivity. However, there are few reports on the selectivity of FIH for the hydroxylation of specific residues. Here, we report that histidinyl residues within the ankrin repeat domain of tankyrase-2 can be hydroxlated by FIH NMR and crystallographic analyses show that the histidinyl hydroxylation occurs at the beta-position. The results further expand the scope of FIH-catalysed hydroxylations.
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