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| {{STRUCTURE_2gp5| PDB=2gp5 | SCENE= }} | | {{STRUCTURE_2gp5| PDB=2gp5 | SCENE= }} |
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| '''Crystal structure of catalytic core domain of jmjd2A complexed with alpha-Ketoglutarate'''
| | ===Crystal structure of catalytic core domain of jmjd2A complexed with alpha-Ketoglutarate=== |
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| ==Overview==
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| Posttranslational modifications of histones regulate chromatin structure and gene expression. Histone demethylases, members of a newly emerging transcription-factor family, remove methyl groups from the lysine residues of the histone tails and thereby regulate the transcriptional activity of target genes. JmjC-domain-containing proteins have been predicted to be demethylases. For example, the JmjC-containing protein JMJD2A has been characterized as a H3-K9me3- and H3-K36me3-specific demethylase. Here, structures of the catalytic-core domain of JMJD2A with and without alpha-ketoglutarate in the presence of Fe2+ have been determined by X-ray crystallography. The structure of the core domain, consisting of the JmjN domain, the JmjC domain, the C-terminal domain, and a zinc-finger motif, revealed the unique elements that form a potential substrate binding pocket. Sited-directed mutagenesis in conjunction with demethylase activity assays allowed us to propose a molecular model for substrate selection by the JMJD2 histone demethylase family.
| | The line below this paragraph, {{ABSTRACT_PUBMED_16677698}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 16677698 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_16677698}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Metal binding protein]] | | [[Category: Metal binding protein]] |
| [[Category: Zinc finger]] | | [[Category: Zinc finger]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu May 22 22:24:00 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 05:14:33 2008'' |