1jjs
From Proteopedia
(New page: 200px<br /><applet load="1jjs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jjs" /> '''NMR Structure of IBiD, A Domain of CBP/p300'...) |
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'''NMR Structure of IBiD, A Domain of CBP/p300'''<br /> | '''NMR Structure of IBiD, A Domain of CBP/p300'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The transcriptional coactivators CBP and p300 are critical regulators of | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1JJS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http:// | + | 1JJS is a [http://en.wikipedia.org/wiki/Single_protein 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]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Fraenkel, E.]] | [[Category: Fraenkel, E.]] | ||
| - | [[Category: Hare, B | + | [[Category: Hare, B J.]] |
| - | [[Category: Harrison, S | + | [[Category: Harrison, S C.]] |
| - | [[Category: Lin, C | + | [[Category: Lin, C H.]] |
[[Category: Maniatis, T.]] | [[Category: Maniatis, T.]] | ||
[[Category: Wagner, G.]] | [[Category: Wagner, G.]] | ||
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[[Category: transcription regulation]] | [[Category: transcription regulation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:23:28 2008'' |
Revision as of 11:23, 21 February 2008
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NMR Structure of IBiD, A Domain of CBP/p300
Overview
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.
About this Structure
1JJS is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
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
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