2k8f

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{{Seed}}
 
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[[Image:2k8f.jpg|left|200px]]
 
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==Structural Basis for the Regulation of p53 Function by p300==
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The line below this paragraph, containing "STRUCTURE_2k8f", creates the "Structure Box" on the page.
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<StructureSection load='2k8f' size='340' side='right'caption='[[2k8f]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2k8f]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K8F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K8F FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2k8f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k8f OCA], [https://pdbe.org/2k8f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k8f RCSB], [https://www.ebi.ac.uk/pdbsum/2k8f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k8f ProSAT]</span></td></tr>
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{{STRUCTURE_2k8f| PDB=2k8f | SCENE= }}
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/EP300_HUMAN EP300_HUMAN] Note=Defects in EP300 may play a role in epithelial cancer. Note=Chromosomal aberrations involving EP300 may be a cause of acute myeloid leukemias. Translocation t(8;22)(p11;q13) with KAT6A. Defects in EP300 are the cause of Rubinstein-Taybi syndrome type 2 (RSTS2) [MIM:[https://omim.org/entry/613684 613684]. A disorder characterized by craniofacial abnormalities, postnatal growth deficiency, broad thumbs, broad big toes, mental retardation and a propensity for development of malignancies. Some individuals with RSTS2 have less severe mental impairment, more severe microcephaly, and a greater degree of changes in facial bone structure than RSTS1 patients.<ref>PMID:15706485</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/EP300_HUMAN EP300_HUMAN] Functions as histone acetyltransferase and regulates transcription via chromatin remodeling. Acetylates all four core histones in nucleosomes. Histone acetylation gives an epigenetic tag for transcriptional activation. Mediates cAMP-gene regulation by binding specifically to phosphorylated CREB protein. Also functions as acetyltransferase for nonhistone targets. Acetylates 'Lys-131' of ALX1 and acts as its coactivator in the presence of CREBBP. Acetylates SIRT2 and is proposed to indirectly increase the transcriptional activity of TP53 through acetylation and subsequent attenuation of SIRT2 deacetylase function. Acetylates HDAC1 leading to its inactivation and modulation of transcription. Acts as a TFAP2A-mediated transcriptional coactivator in presence of CITED2. Plays a role as a coactivator of NEUROD1-dependent transcription of the secretin and p21 genes and controls terminal differentiation of cells in the intestinal epithelium. Promotes cardiac myocyte enlargement. Can also mediate transcriptional repression. Binds to and may be involved in the transforming capacity of the adenovirus E1A protein. In case of HIV-1 infection, it is recruited by the viral protein Tat. Regulates Tat's transactivating activity and may help inducing chromatin remodeling of proviral genes. Acetylates FOXO1 and enhances its transcriptional activity.<ref>PMID:11701890</ref> <ref>PMID:10733570</ref> <ref>PMID:11430825</ref> <ref>PMID:12586840</ref> <ref>PMID:12929931</ref> <ref>PMID:15186775</ref> <ref>PMID:15890677</ref> <ref>PMID:16762839</ref> <ref>PMID:18722353</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k8/2k8f_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2k8f ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Coactivators CREB-binding protein and p300 play important roles in mediating the transcriptional activity of p53. Until now, however, no detailed structural information has been available on how any of the domains of p300 interact with p53. Here, we report the NMR structure of the complex of the Taz2 (C/H3) domain of p300 and the N-terminal transactivation domain of p53. In the complex, p53 forms a short alpha helix and interacts with the Taz2 domain through an extended surface. Mutational analyses demonstrate the importance of hydrophobic residues for complex stabilization. Additionally, they suggest that the increased affinity of Taz2 for p53(1-39) phosphorylated at Thr(18) is due in part to electrostatic interactions of the phosphate with neighboring arginine residues in Taz2. Thermodynamic experiments revealed the importance of hydrophobic interactions in the complex of Taz2 with p53 phosphorylated at Ser(15) and Thr(18).
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===Structural Basis for the Regulation of p53 Function by p300===
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Structural basis for p300 Taz2-p53 TAD1 binding and modulation by phosphorylation.,Feng H, Jenkins LM, Durell SR, Hayashi R, Mazur SJ, Cherry S, Tropea JE, Miller M, Wlodawer A, Appella E, Bai Y Structure. 2009 Feb 13;17(2):202-10. PMID:19217391<ref>PMID:19217391</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2k8f" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_19217391}}, adds the Publication Abstract to the page
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*[[Histone acetyltransferase 3D structures|Histone acetyltransferase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 19217391 is the PubMed ID number.
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*[[P53 3D structures|P53 3D structures]]
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== References ==
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{{ABSTRACT_PUBMED_19217391}}
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<references/>
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__TOC__
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==About this Structure==
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</StructureSection>
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2K8F is a 2 chains 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=2K8F OCA].
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==Reference==
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<ref group="xtra">PMID:19217391</ref><references group="xtra"/>
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[[Category: Histone acetyltransferase]]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Appella, E.]]
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[[Category: Large Structures]]
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[[Category: Bai, Y.]]
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[[Category: Appella E]]
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[[Category: Durell, S R.]]
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[[Category: Bai Y]]
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[[Category: Feng, H.]]
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[[Category: Durell SR]]
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[[Category: Jenkins, L M.]]
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[[Category: Feng H]]
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[[Category: Wiodawer, A.]]
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[[Category: Jenkins LM]]
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[[Category: Acetylation]]
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[[Category: Wiodawer A]]
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[[Category: Activator]]
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[[Category: Alternative splicing]]
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[[Category: Anti-oncogene]]
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[[Category: Apoptosis]]
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[[Category: Bromodomain]]
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[[Category: Cell cycle]]
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[[Category: Chromosomal rearrangement]]
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[[Category: Citrullination]]
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[[Category: Complex of p53 and p300]]
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[[Category: Covalent protein-rna linkage]]
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[[Category: Cytoplasm]]
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[[Category: Disease mutation]]
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[[Category: Dna-binding]]
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[[Category: Endoplasmic reticulum]]
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[[Category: Glycoprotein]]
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[[Category: Host-virus interaction]]
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[[Category: Li-fraumeni syndrome]]
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[[Category: Metal-binding]]
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[[Category: Methylation]]
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[[Category: Nucleus]]
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[[Category: Phosphoprotein]]
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[[Category: Polymorphism]]
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[[Category: Transcription]]
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[[Category: Transcription regulation]]
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[[Category: Transferase]]
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[[Category: Transferase/transcription complex]]
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[[Category: Ubl conjugation]]
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[[Category: Zinc]]
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[[Category: Zinc-finger]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 4 14:28:48 2009''
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Current revision

Structural Basis for the Regulation of p53 Function by p300

PDB ID 2k8f

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