1jjs

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[[Image:1jjs.jpg|left|200px]]
 
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{{Structure
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==NMR Structure of IBiD, A Domain of CBP/p300==
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|PDB= 1jjs |SIZE=350|CAPTION= <scene name='initialview01'>1jjs</scene>
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<StructureSection load='1jjs' size='340' side='right'caption='[[1jjs]]' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1jjs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JJS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JJS FirstGlance]. <br>
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|ACTIVITY=
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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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|GENE= CBP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
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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=1jjs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jjs OCA], [https://pdbe.org/1jjs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jjs RCSB], [https://www.ebi.ac.uk/pdbsum/1jjs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jjs ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jjs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jjs OCA], [http://www.ebi.ac.uk/pdbsum/1jjs PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jjs RCSB]</span>
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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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}}
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The transcriptional coactivators CBP and p300 are critical regulators of metazoan gene expression. They associate with many different DNA-bound transcription factors through small, conserved domains. We have identified a compactly folded 46 residue domain in CBP and p300, the IRF-3 binding domain (IBiD), and we have determined its structure by NMR. It has a helical framework containing an apparently flexible polyglutamine loop that participates in ligand binding. Spectroscopic data indicate that induced folding accompanies association of IBiD with its partners, which exhibit no evident sequence similarities. We demonstrate the significance both in vitro and in vivo of interactions between IBiD and a number of diverse partners. Thus, IBiD is an important contributor to signal integration by CBP and p300.
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'''NMR Structure of IBiD, A Domain of CBP/p300'''
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A small domain of CBP/p300 binds diverse proteins: solution structure and functional studies.,Lin CH, Hare BJ, Wagner G, Harrison SC, Maniatis T, Fraenkel E Mol Cell. 2001 Sep;8(3):581-90. PMID:11583620<ref>PMID:11583620</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 1jjs" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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The transcriptional coactivators CBP and p300 are critical regulators of metazoan gene expression. They associate with many different DNA-bound transcription factors through small, conserved domains. We have identified a compactly folded 46 residue domain in CBP and p300, the IRF-3 binding domain (IBiD), and we have determined its structure by NMR. It has a helical framework containing an apparently flexible polyglutamine loop that participates in ligand binding. Spectroscopic data indicate that induced folding accompanies association of IBiD with its partners, which exhibit no evident sequence similarities. We demonstrate the significance both in vitro and in vivo of interactions between IBiD and a number of diverse partners. Thus, IBiD is an important contributor to signal integration by CBP and p300.
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*[[CREB-binding protein 3D structures|CREB-binding protein 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1JJS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JJS OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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A small domain of CBP/p300 binds diverse proteins: solution structure and functional studies., Lin CH, Hare BJ, Wagner G, Harrison SC, Maniatis T, Fraenkel E, Mol Cell. 2001 Sep;8(3):581-90. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11583620 11583620]
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Single protein]]
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[[Category: Fraenkel E]]
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[[Category: Fraenkel, E.]]
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[[Category: Hare BJ]]
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[[Category: Hare, B J.]]
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[[Category: Harrison SC]]
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[[Category: Harrison, S C.]]
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[[Category: Lin CH]]
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[[Category: Lin, C H.]]
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[[Category: Maniatis T]]
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[[Category: Maniatis, T.]]
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[[Category: Wagner G]]
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[[Category: Wagner, G.]]
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[[Category: coactivator]]
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[[Category: transcription regulation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:34:40 2008''
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Current revision

NMR Structure of IBiD, A Domain of CBP/p300

PDB ID 1jjs

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