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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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Publisher copy:
10.1016/j.jmb.2010.05.054

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Journal:
Journal of molecular biology
Publication date:
2010-05-05
DOI:
EISSN:
1089-8638
ISSN:
0022-2836
URN:
uuid:ca0610df-140e-4d00-8519-12f7095ef507
Source identifiers:
124662
Local pid:
pubs:124662
Language:
English

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