2rny

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{{Seed}}
 
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[[Image:2rny.png|left|200px]]
 
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==Complex Structures of CBP Bromodomain with H4 ack20 Peptide==
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The line below this paragraph, containing "STRUCTURE_2rny", creates the "Structure Box" on the page.
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<StructureSection load='2rny' size='340' side='right'caption='[[2rny]]' 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'>[[2rny]] 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=2RNY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RNY 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, 20 models</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ALY:N(6)-ACETYLLYSINE'>ALY</scene></td></tr>
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{{STRUCTURE_2rny| PDB=2rny | SCENE= }}
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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=2rny FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rny OCA], [https://pdbe.org/2rny PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rny RCSB], [https://www.ebi.ac.uk/pdbsum/2rny PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rny ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/CBP_HUMAN CBP_HUMAN] Note=Chromosomal aberrations involving CREBBP may be a cause of acute myeloid leukemias. Translocation t(8;16)(p11;p13) with KAT6A; translocation t(11;16)(q23;p13.3) with MLL/HRX; translocation t(10;16)(q22;p13) with KAT6B. KAT6A-CREBBP may induce leukemia by inhibiting RUNX1-mediated transcription. Defects in CREBBP are a cause of Rubinstein-Taybi syndrome type 1 (RSTS1) [MIM:[https://omim.org/entry/180849 180849]. RSTS1 is an autosomal dominant disorder characterized by craniofacial abnormalities, broad thumbs, broad big toes, mental retardation and a propensity for development of malignancies.<ref>PMID:11331617</ref> <ref>PMID:12114483</ref> <ref>PMID:12566391</ref> <ref>PMID:15706485</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/CBP_HUMAN CBP_HUMAN] Acetylates histones, giving a specific tag for transcriptional activation. Also acetylates non-histone proteins, like NCOA3 and FOXO1. Binds specifically to phosphorylated CREB and enhances its transcriptional activity toward cAMP-responsive genes. Acts as a coactivator of ALX1 in the presence of EP300.<ref>PMID:9707565</ref> <ref>PMID:11154691</ref> <ref>PMID:12738767</ref> <ref>PMID:12929931</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/rn/2rny_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2rny 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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Histone lysine acetylation is central to epigenetic control of gene transcription. Bromodomains of chromosomal proteins function as acetyl-lysine (Kac) binding domains. However, how bromodomains recognize site-specific histones remains unanswered. Here, we report three three-dimensional solution structures of the bromodomains of the human transcriptional coactivators CREB-binding protein (CBP) and p300/CBP-associated factor (PCAF) bound to peptides derived from histone acetylation sites at lysines 36 and 9 in H3, and lysine 20 in H4. From structural and biochemical binding analyses, we determine consensus histone recognition by the bromodomains of PCAF and CBP, which represent two different subgroups of the bromodomain family. Through bromodomain residues in the ZA and BC loops, PCAF prefers acetylation sites with a hydrophobic residue at (Kac+2) position and a positively charged or aromatic residue at (Kac+3), whereas CBP favors bulky hydrophobic residues at (Kac+1) and (Kac+2), a positively charged residue at (Kac-1), and an aromatic residue at (Kac-2).
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===Complex Structures of CBP Bromodomain with H4 ack20 Peptide===
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Structural basis of site-specific histone recognition by the bromodomains of human coactivators PCAF and CBP/p300.,Zeng L, Zhang Q, Gerona-Navarro G, Moshkina N, Zhou MM Structure. 2008 Apr;16(4):643-52. PMID:18400184<ref>PMID:18400184</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 2rny" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_18400184}}, adds the Publication Abstract to the page
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*[[CREB-binding protein 3D structures|CREB-binding protein 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 18400184 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_18400184}}
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__TOC__
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</StructureSection>
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==About this Structure==
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2RNY is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RNY OCA].
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==Reference==
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Structural Basis of Site-Specific Histone Recognition by the Bromodomains of Human Coactivators PCAF and CBP/p300., Zeng L, Zhang Q, Gerona-Navarro G, Moshkina N, Zhou MM, Structure. 2008 Apr;16(4):643-52. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18400184 18400184]
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[[Category: Histone acetyltransferase]]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Gerona-Navarro, G.]]
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[[Category: Gerona-Navarro G]]
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[[Category: Zeng, L.]]
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[[Category: Zeng L]]
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[[Category: Zhang, Q.]]
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[[Category: Zhang Q]]
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[[Category: Zhou, M M.]]
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[[Category: Zhou MM]]
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[[Category: Acetylation]]
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[[Category: Activator]]
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[[Category: Bromodomain]]
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[[Category: Cbp]]
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[[Category: Chromosomal protein]]
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[[Category: Chromosomal rearrangement]]
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[[Category: Creb]]
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[[Category: Disease mutation]]
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[[Category: Dna-binding]]
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[[Category: Histone]]
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[[Category: Host-virus interaction]]
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[[Category: Metal-binding]]
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[[Category: Methylation]]
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[[Category: Nucleosome core]]
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[[Category: Nucleus]]
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[[Category: P53]]
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[[Category: Phosphoprotein]]
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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/nuclear protein complex]]
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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 Mon Jul 28 08:29:25 2008''
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Current revision

Complex Structures of CBP Bromodomain with H4 ack20 Peptide

PDB ID 2rny

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