View source for 1jjs


==NMR Structure of IBiD, A Domain of CBP/p300==
<StructureSection load='1jjs' size='340' side='right'caption='[[1jjs]]' scene=''>
== Structural highlights ==
<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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=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>
</table>
== Function ==
[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> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1jjs" style="background-color:#fffaf0;"></div>

==See Also==
*[[CREB-binding protein 3D structures|CREB-binding protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Fraenkel E]]
[[Category: Hare BJ]]
[[Category: Harrison SC]]
[[Category: Lin CH]]
[[Category: Maniatis T]]
[[Category: Wagner G]]