2c1n
From Proteopedia
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- | [[Image:2c1n.png|left|200px]] | ||
- | + | ==Molecular basis for the recognition of phosphorylated and phosphoacetylated histone H3 by 14-3-3== | |
- | + | <StructureSection load='2c1n' size='340' side='right'caption='[[2c1n]], [[Resolution|resolution]] 2.00Å' scene=''> | |
- | + | == Structural highlights == | |
- | or the | + | <table><tr><td colspan='2'>[[2c1n]] is a 4 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C1N FirstGlance]. <br> |
- | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | |
- | - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr> |
- | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2c1n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c1n OCA], [https://pdbe.org/2c1n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c1n RCSB], [https://www.ebi.ac.uk/pdbsum/2c1n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c1n ProSAT]</span></td></tr> | |
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/1433Z_HUMAN 1433Z_HUMAN] Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner.<ref>PMID:9360956</ref> <ref>PMID:14578935</ref> <ref>PMID:15071501</ref> <ref>PMID:15644438</ref> <ref>PMID:16376338</ref> | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c1/2c1n_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2c1n ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | 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. | ||
- | + | 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<ref>PMID:16246723</ref> | |
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 2c1n" style="background-color:#fffaf0;"></div> | ||
- | + | ==See Also== | |
- | + | *[[14-3-3 protein 3D structures|14-3-3 protein 3D structures]] | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
- | == | + | |
- | [[ | + | |
- | + | ||
- | == | + | |
- | < | + | |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
- | [[Category: Clayton | + | [[Category: Large Structures]] |
- | [[Category: Clynes | + | [[Category: Clayton AL]] |
- | [[Category: Edmunds | + | [[Category: Clynes D]] |
- | [[Category: Endicott | + | [[Category: Edmunds JW]] |
- | [[Category: Macdonald | + | [[Category: Endicott JA]] |
- | [[Category: Mahadevan | + | [[Category: Macdonald N]] |
- | [[Category: Moggs | + | [[Category: Mahadevan LC]] |
- | [[Category: Nguyen | + | [[Category: Moggs JG]] |
- | [[Category: Noble | + | [[Category: Nguyen A]] |
- | [[Category: Orphanides | + | [[Category: Noble MEM]] |
- | [[Category: Thomson | + | [[Category: Orphanides G]] |
- | [[Category: Welburn | + | [[Category: Thomson S]] |
- | [[Category: Yaffe | + | [[Category: Welburn JPI]] |
- | + | [[Category: Yaffe MB]] | |
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- | + | ||
- | + |
Current revision
Molecular basis for the recognition of phosphorylated and phosphoacetylated histone H3 by 14-3-3
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Categories: Homo sapiens | Large Structures | Clayton AL | Clynes D | Edmunds JW | Endicott JA | Macdonald N | Mahadevan LC | Moggs JG | Nguyen A | Noble MEM | Orphanides G | Thomson S | Welburn JPI | Yaffe MB