2c1n

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(New page: 200px<br /> <applet load="2c1n" size="450" color="white" frame="true" align="right" spinBox="true" caption="2c1n, resolution 2.00&Aring;" /> '''MOLECULAR BASIS FOR...)
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[[Image:2c1n.gif|left|200px]]<br />
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[[Image:2c1n.gif|left|200px]]<br /><applet load="2c1n" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="2c1n" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="2c1n, resolution 2.00&Aring;" />
caption="2c1n, resolution 2.00&Aring;" />
'''MOLECULAR BASIS FOR THE RECOGNITION OF PHOSPHORYLATED AND PHOSPHOACETYLATED HISTONE H3 BY 14-3-3'''<br />
'''MOLECULAR BASIS FOR THE RECOGNITION OF PHOSPHORYLATED AND PHOSPHOACETYLATED HISTONE H3 BY 14-3-3'''<br />
==Overview==
==Overview==
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Phosphorylation of histone H3 is implicated in transcriptional activation, and chromosome condensation, but its immediate molecular function has, remained obscure. By affinity chromatography of nuclear extracts against, modified H3 tail peptides, we identified 14-3-3 isoforms as proteins that, bind these tails in a strictly phosphorylation-dependent manner., Acetylation of lysines 9 and 14 does not impede 14-3-3 binding to serine, 10-phosphorylated H3 tails. In vivo, 14-3-3 is inducibly recruited to, c-fos and c-jun nucleosomes upon gene activation, concomitant with H3, phosphoacetylation. We have determined the structures of 14-3-3zeta, complexed with serine 10-phosphorylated or phosphoacetylated H3 peptides., These reveal a distinct mode of 14-3-3/phosphopeptide binding and provide, a structural understanding for the lack of effect of acetylation at, lysines 9 and 14 on this interaction. 14-3-3 isoforms thus represent a, class of proteins that mediate the effect of histone phosphorylation at, inducible genes.
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Phosphorylation of histone H3 is implicated in transcriptional activation and chromosome condensation, but its immediate molecular function has remained obscure. By affinity chromatography of nuclear extracts against modified H3 tail peptides, we identified 14-3-3 isoforms as proteins that bind these tails in a strictly phosphorylation-dependent manner. Acetylation of lysines 9 and 14 does not impede 14-3-3 binding to serine 10-phosphorylated H3 tails. In vivo, 14-3-3 is inducibly recruited to c-fos and c-jun nucleosomes upon gene activation, concomitant with H3 phosphoacetylation. We have determined the structures of 14-3-3zeta complexed with serine 10-phosphorylated or phosphoacetylated H3 peptides. These reveal a distinct mode of 14-3-3/phosphopeptide binding and provide a structural understanding for the lack of effect of acetylation at lysines 9 and 14 on this interaction. 14-3-3 isoforms thus represent a class of proteins that mediate the effect of histone phosphorylation at inducible genes.
==About this Structure==
==About this Structure==
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2C1N is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2C1N OCA].
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2C1N is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C1N OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Clayton, A.L.]]
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[[Category: Clayton, A L.]]
[[Category: Clynes, D.]]
[[Category: Clynes, D.]]
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[[Category: Edmunds, J.W.]]
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[[Category: Edmunds, J W.]]
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[[Category: Endicott, J.A.]]
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[[Category: Endicott, J A.]]
[[Category: Macdonald, N.]]
[[Category: Macdonald, N.]]
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[[Category: Mahadevan, L.C.]]
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[[Category: Mahadevan, L C.]]
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[[Category: Moggs, J.G.]]
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[[Category: Moggs, J G.]]
[[Category: Nguyen, A.]]
[[Category: Nguyen, A.]]
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[[Category: Noble, M.E.M.]]
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[[Category: Noble, M E.M.]]
[[Category: Orphanides, G.]]
[[Category: Orphanides, G.]]
[[Category: Thomson, S.]]
[[Category: Thomson, S.]]
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[[Category: Welburn, J.P.I.]]
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[[Category: Welburn, J P.I.]]
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[[Category: Yaffe, M.B.]]
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[[Category: Yaffe, M B.]]
[[Category: 14-3-3]]
[[Category: 14-3-3]]
[[Category: acetylation]]
[[Category: acetylation]]
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[[Category: signaling protein]]
[[Category: signaling protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 21:09:38 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:43:55 2008''

Revision as of 14:43, 21 February 2008


2c1n, resolution 2.00Å

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MOLECULAR BASIS FOR THE RECOGNITION OF PHOSPHORYLATED AND PHOSPHOACETYLATED HISTONE H3 BY 14-3-3

Overview

Phosphorylation of histone H3 is implicated in transcriptional activation and chromosome condensation, but its immediate molecular function has remained obscure. By affinity chromatography of nuclear extracts against modified H3 tail peptides, we identified 14-3-3 isoforms as proteins that bind these tails in a strictly phosphorylation-dependent manner. Acetylation of lysines 9 and 14 does not impede 14-3-3 binding to serine 10-phosphorylated H3 tails. In vivo, 14-3-3 is inducibly recruited to c-fos and c-jun nucleosomes upon gene activation, concomitant with H3 phosphoacetylation. We have determined the structures of 14-3-3zeta complexed with serine 10-phosphorylated or phosphoacetylated H3 peptides. These reveal a distinct mode of 14-3-3/phosphopeptide binding and provide a structural understanding for the lack of effect of acetylation at lysines 9 and 14 on this interaction. 14-3-3 isoforms thus represent a class of proteins that mediate the effect of histone phosphorylation at inducible genes.

About this Structure

2C1N is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Molecular basis for the recognition of phosphorylated and phosphoacetylated histone h3 by 14-3-3., Macdonald N, Welburn JP, Noble ME, Nguyen A, Yaffe MB, Clynes D, Moggs JG, Orphanides G, Thomson S, Edmunds JW, Clayton AL, Endicott JA, Mahadevan LC, Mol Cell. 2005 Oct 28;20(2):199-211. PMID:16246723

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