2c1n
From Proteopedia
Line 1: | Line 1: | ||
- | [[Image:2c1n.gif|left|200px]] | + | [[Image:2c1n.gif|left|200px]] |
- | + | ||
- | '''MOLECULAR BASIS FOR THE RECOGNITION OF PHOSPHORYLATED AND PHOSPHOACETYLATED HISTONE H3 BY 14-3-3''' | + | {{Structure |
+ | |PDB= 2c1n |SIZE=350|CAPTION= <scene name='initialview01'>2c1n</scene>, resolution 2.00Å | ||
+ | |SITE= | ||
+ | |LIGAND= | ||
+ | |ACTIVITY= | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''MOLECULAR BASIS FOR THE RECOGNITION OF PHOSPHORYLATED AND PHOSPHOACETYLATED HISTONE H3 BY 14-3-3''' | ||
+ | |||
==Overview== | ==Overview== | ||
Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
- | 2C1N is a [ | + | 2C1N is a [[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== | ||
- | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16246723 16246723] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
Line 33: | Line 42: | ||
[[Category: signaling protein]] | [[Category: signaling protein]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:09:35 2008'' |
Revision as of 14:09, 20 March 2008
| |||||||
, resolution 2.00Å | |||||||
---|---|---|---|---|---|---|---|
Coordinates: | save as pdb, mmCIF, xml |
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
Page seeded by OCA on Thu Mar 20 16:09:35 2008
Categories: Homo sapiens | Protein complex | Clayton, A L. | Clynes, D. | Edmunds, J W. | Endicott, J A. | Macdonald, N. | Mahadevan, L C. | Moggs, J G. | Nguyen, A. | Noble, M E.M. | Orphanides, G. | Thomson, S. | Welburn, J P.I. | Yaffe, M B. | 14-3-3 | Acetylation | Histone h3 | Nucleosome | Phosphorylation | Signaling protein