2pxj

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==Overview==
==Overview==
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The Jumonji C domain is a catalytic motif that mediates histone lysine, demethylation. The Jumonji C-containing oxygenase JMJD2A specifically, demethylates tri- and dimethylated lysine-9 and lysine-36 of histone 3, (H3K9/36me3/2). Here we present structures of the JMJD2A catalytic core, complexed with methylated H3K36 peptide substrates in the presence of, Fe(II) and N-oxalylglycine. We found that the interaction between JMJD2A, and peptides largely involves the main chains of the enzyme and the, peptide. The peptide-binding specificity is primarily determined by the, primary structure of the peptide, which explains the specificity of JMJD2A, for methylated H3K9 and H3K36 instead of other methylated residues such as, H3K27. The specificity for a particular methyl group, however, is affected, by multiple factors, such as space and the electrostatic environment in, the catalytic center of the enzyme. These results provide insights into, the mechanisms and specificity of histone demethylation.
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The Jumonji C domain is a catalytic motif that mediates histone lysine demethylation. The Jumonji C-containing oxygenase JMJD2A specifically demethylates tri- and dimethylated lysine-9 and lysine-36 of histone 3 (H3K9/36 me3/2). Here we present structures of the JMJD2A catalytic core complexed with methylated H3K36 peptide substrates in the presence of Fe(II) and N-oxalylglycine. We found that the interaction between JMJD2A and peptides largely involves the main chains of the enzyme and the peptide. The peptide-binding specificity is primarily determined by the primary structure of the peptide, which explains the specificity of JMJD2A for methylated H3K9 and H3K36 instead of other methylated residues such as H3K27. The specificity for a particular methyl group, however, is affected by multiple factors, such as space and the electrostatic environment in the catalytic center of the enzyme. These results provide insights into the mechanisms and specificity of histone demethylation.
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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Structural basis of the recognition of a methylated histone tail by JMJD2A., Chen Z, Zang J, Kappler J, Hong X, Crawford F, Wang Q, Lan F, Jiang C, Whetstine J, Dai S, Hansen K, Shi Y, Zhang G, Proc Natl Acad Sci U S A. 2007 Jun 13;. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17567753 17567753]
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Structural basis of the recognition of a methylated histone tail by JMJD2A., Chen Z, Zang J, Kappler J, Hong X, Crawford F, Wang Q, Lan F, Jiang C, Whetstine J, Dai S, Hansen K, Shi Y, Zhang G, Proc Natl Acad Sci U S A. 2007 Jun 26;104(26):10818-23. Epub 2007 Jun 13. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17567753 17567753]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: jmjd2a; histone demethylase; jmjc; h3k36]]
[[Category: jmjd2a; histone demethylase; jmjc; h3k36]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:43:55 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:34:03 2008''

Revision as of 16:34, 21 February 2008


2pxj, resolution 2.00Å

Drag the structure with the mouse to rotate

The complex structure of JMJD2A and monomethylated H3K36 peptide

Overview

The Jumonji C domain is a catalytic motif that mediates histone lysine demethylation. The Jumonji C-containing oxygenase JMJD2A specifically demethylates tri- and dimethylated lysine-9 and lysine-36 of histone 3 (H3K9/36 me3/2). Here we present structures of the JMJD2A catalytic core complexed with methylated H3K36 peptide substrates in the presence of Fe(II) and N-oxalylglycine. We found that the interaction between JMJD2A and peptides largely involves the main chains of the enzyme and the peptide. The peptide-binding specificity is primarily determined by the primary structure of the peptide, which explains the specificity of JMJD2A for methylated H3K9 and H3K36 instead of other methylated residues such as H3K27. The specificity for a particular methyl group, however, is affected by multiple factors, such as space and the electrostatic environment in the catalytic center of the enzyme. These results provide insights into the mechanisms and specificity of histone demethylation.

About this Structure

2PXJ is a Single protein structure of sequence from Homo sapiens with , and as ligands. Full crystallographic information is available from OCA.

Reference

Structural basis of the recognition of a methylated histone tail by JMJD2A., Chen Z, Zang J, Kappler J, Hong X, Crawford F, Wang Q, Lan F, Jiang C, Whetstine J, Dai S, Hansen K, Shi Y, Zhang G, Proc Natl Acad Sci U S A. 2007 Jun 26;104(26):10818-23. Epub 2007 Jun 13. PMID:17567753

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