2gp5: Difference between revisions

Revision as of 05:14, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2gp5.png

Template:STRUCTURE 2gp5

Crystal structure of catalytic core domain of jmjd2A complexed with alpha-KetoglutarateCrystal structure of catalytic core domain of jmjd2A complexed with alpha-Ketoglutarate

Template:ABSTRACT PUBMED 16677698

About this StructureAbout this Structure

2GP5 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Structural insights into histone demethylation by JMJD2 family members., Chen Z, Zang J, Whetstine J, Hong X, Davrazou F, Kutateladze TG, Simpson M, Mao Q, Pan CH, Dai S, Hagman J, Hansen K, Shi Y, Zhang G, Cell. 2006 May 19;125(4):691-702. Epub 2006 May 4. PMID:16677698

Page seeded by OCA on Mon Jul 28 05:14:33 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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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===
-==Overview==
+<!--
-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
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+{{ABSTRACT_PUBMED_16677698}}
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 [[Category: Metal binding protein]]
 [[Category: Zinc finger]]
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