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Crystal structure of the 2-oxoglutarate- and Fe(II)-dependent lysyl hydroxylase JMJD6.

Abstract:

Lysyl and prolyl hydroxylations are well-known post-translational modifications to animal and plant proteins with extracellular roles. More recent work has indicated that the hydroxylation of intracellular animal proteins may be common. JMJD6 catalyses the iron- and 2-oxoglutarate-dependent hydroxylation of lysyl residues in arginine-serine-rich domains of RNA splicing-related proteins. We report crystallographic studies on the catalytic domain of JMJD6 in complex with Ni(II) substituting for...

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Publication status:
Published

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Publisher copy:
10.1016/j.jmb.2010.05.054

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Journal:
Journal of molecular biology
Volume:
401
Issue:
2
Pages:
211-222
Publication date:
2010-08-05
DOI:
EISSN:
1089-8638
ISSN:
0022-2836
URN:
uuid:8a0a610a-48ff-4d42-86d4-cd64e6b262e4
Source identifiers:
66097
Local pid:
pubs:66097

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