2c52

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{{Seed}}
 
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[[Image:2c52.png|left|200px]]
 
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==Structural diversity in CBP p160 complexes==
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The line below this paragraph, containing "STRUCTURE_2c52", creates the "Structure Box" on the page.
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<StructureSection load='2c52' size='340' side='right'caption='[[2c52]]' 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'>[[2c52]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C52 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C52 FirstGlance]. <br>
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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=2c52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c52 OCA], [https://pdbe.org/2c52 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c52 RCSB], [https://www.ebi.ac.uk/pdbsum/2c52 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c52 ProSAT]</span></td></tr>
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{{STRUCTURE_2c52| PDB=2c52 | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CBP_MOUSE CBP_MOUSE] 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 (By similarity).<ref>PMID:10207073</ref> <ref>PMID:11701890</ref> <ref>PMID:15220471</ref> <ref>PMID:16287980</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/c5/2c52_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=2c52 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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Ligand-induced transcription by nuclear receptors involves the recruitment of p160 coactivators such as steroid receptor coactivator 1 (SRC1), in complex with histone acetyltransferases such as CREB-binding protein (CBP) and p300. Here we describe the solution structure of a complex formed by the SRC1 interaction domain (SID) of CBP and the activation domain (AD1) of SRC1, both of which contain four helical regions (Calpha1, Calpha2, Calpha3, and Calpha3' in CBP and Salpha1, Salpha2', Salpha2, and Salpha3 in SRC1). A tight four-helix bundle is formed between Salpha1, Calpha1, Calpha2, and Calpha3 that is capped by Salpha3. In contrast to the structure of the AD1 domain of the related p160 protein ACTR in complex with CBP SID, the sequences forming Salpha2' and Salpha2 in SRC1 AD1 are not involved in the interface between the two domains but rather serve to position Salpha3. Thus, although the CBP SID domain adopts a similar fold in complex with different p160 proteins, the topologies of the AD1 domains are strikingly different, a feature that is likely to contribute to functional specificity of these coactivator complexes.
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===STRUCTURAL DIVERSITY IN CBP P160 COMPLEXES===
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Structural diversity in p160/CREB-binding protein coactivator complexes.,Waters L, Yue B, Veverka V, Renshaw P, Bramham J, Matsuda S, Frenkiel T, Kelly G, Muskett F, Carr M, Heery DM J Biol Chem. 2006 May 26;281(21):14787-95. Epub 2006 Mar 15. PMID:16540468<ref>PMID:16540468</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 2c52" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_16540468}}, 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 16540468 is the PubMed ID number.
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*[[Nuclear receptor coactivator|Nuclear receptor coactivator]]
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== References ==
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{{ABSTRACT_PUBMED_16540468}}
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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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2C52 is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C52 OCA].
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==Reference==
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<ref group="xtra">PMID:16540468</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: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Bramham, J.]]
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[[Category: Bramham J]]
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[[Category: Carr, M D.]]
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[[Category: Carr MD]]
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[[Category: Frenkiel, T.]]
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[[Category: Frenkiel T]]
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[[Category: Heery, D M.]]
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[[Category: Heery DM]]
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[[Category: Kelly, G.]]
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[[Category: Kelly G]]
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[[Category: Matsuda, S.]]
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[[Category: Matsuda S]]
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[[Category: Muskett, F W.]]
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[[Category: Muskett FW]]
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[[Category: Renshaw, P S.]]
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[[Category: Renshaw PS]]
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[[Category: Veverka, V.]]
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[[Category: Veverka V]]
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[[Category: Waters, L C.]]
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[[Category: Waters LC]]
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[[Category: Yue, B.]]
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[[Category: Yue B]]
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[[Category: Activator]]
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[[Category: Acyltransferase]]
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[[Category: Alternative splicing]]
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[[Category: Bromodomain]]
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[[Category: Chromosomal translocation]]
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[[Category: Metal-binding]]
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[[Category: Methylation]]
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[[Category: Nuclear protein]]
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[[Category: Polymorphism]]
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[[Category: Proto-oncogene]]
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[[Category: Transcription]]
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[[Category: Transcription regulation]]
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[[Category: Transferase]]
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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 Tue Feb 17 13:48:08 2009''
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Current revision

Structural diversity in CBP p160 complexes

PDB ID 2c52

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