1t2k

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(New page: 200px<br /> <applet load="1t2k" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t2k, resolution 3.00&Aring;" /> '''Structure Of The DN...)
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<applet load="1t2k" size="450" color="white" frame="true" align="right" spinBox="true"
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'''Structure Of The DNA Binding Domains Of IRF3, ATF-2 and Jun Bound To DNA'''<br />
'''Structure Of The DNA Binding Domains Of IRF3, ATF-2 and Jun Bound To DNA'''<br />
==Overview==
==Overview==
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Transcriptional activation of the interferon-beta (IFN-beta) gene requires, assembly of an enhanceosome containing the transcription factors, ATF-2/c-Jun, IRF-3/IRF-7, NF-kappaB and HMGI(Y). These factors, cooperatively bind a composite DNA site and activate expression of the, IFN-beta gene. The 3.0 A crystal structure of the DNA-binding domains of, ATF-2/c-Jun and two IRF-3 molecules in a complex with 31 base pairs (bp), of the PRDIV-PRDIII region of the IFN-beta enhancer shows that association, of the four proteins with DNA creates a continuous surface for the, recognition of 24 bp. The structure, together with in vitro binding, studies and protein mutagenesis, shows that protein-protein interactions, are not critical for cooperative binding. Instead, cooperativity arises, mainly through nucleotide sequence-dependent structural changes in the DNA, that allow formation of complementary DNA conformations. Because the, binding sites overlap on the enhancer, the unit of recognition is the, entire nucleotide sequence, not the individual subsites.
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Transcriptional activation of the interferon-beta (IFN-beta) gene requires assembly of an enhanceosome containing the transcription factors ATF-2/c-Jun, IRF-3/IRF-7, NF-kappaB and HMGI(Y). These factors cooperatively bind a composite DNA site and activate expression of the IFN-beta gene. The 3.0 A crystal structure of the DNA-binding domains of ATF-2/c-Jun and two IRF-3 molecules in a complex with 31 base pairs (bp) of the PRDIV-PRDIII region of the IFN-beta enhancer shows that association of the four proteins with DNA creates a continuous surface for the recognition of 24 bp. The structure, together with in vitro binding studies and protein mutagenesis, shows that protein-protein interactions are not critical for cooperative binding. Instead, cooperativity arises mainly through nucleotide sequence-dependent structural changes in the DNA that allow formation of complementary DNA conformations. Because the binding sites overlap on the enhancer, the unit of recognition is the entire nucleotide sequence, not the individual subsites.
==About this Structure==
==About this Structure==
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1T2K is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1T2K OCA].
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1T2K is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T2K OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Harrison, S.C.]]
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[[Category: Harrison, S C.]]
[[Category: Maniatis, T.]]
[[Category: Maniatis, T.]]
[[Category: Panne, D.]]
[[Category: Panne, D.]]
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[[Category: transcription]]
[[Category: transcription]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:19:35 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:09:10 2008''

Revision as of 13:09, 21 February 2008


1t2k, resolution 3.00Å

Drag the structure with the mouse to rotate

Structure Of The DNA Binding Domains Of IRF3, ATF-2 and Jun Bound To DNA

Overview

Transcriptional activation of the interferon-beta (IFN-beta) gene requires assembly of an enhanceosome containing the transcription factors ATF-2/c-Jun, IRF-3/IRF-7, NF-kappaB and HMGI(Y). These factors cooperatively bind a composite DNA site and activate expression of the IFN-beta gene. The 3.0 A crystal structure of the DNA-binding domains of ATF-2/c-Jun and two IRF-3 molecules in a complex with 31 base pairs (bp) of the PRDIV-PRDIII region of the IFN-beta enhancer shows that association of the four proteins with DNA creates a continuous surface for the recognition of 24 bp. The structure, together with in vitro binding studies and protein mutagenesis, shows that protein-protein interactions are not critical for cooperative binding. Instead, cooperativity arises mainly through nucleotide sequence-dependent structural changes in the DNA that allow formation of complementary DNA conformations. Because the binding sites overlap on the enhancer, the unit of recognition is the entire nucleotide sequence, not the individual subsites.

About this Structure

1T2K is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of ATF-2/c-Jun and IRF-3 bound to the interferon-beta enhancer., Panne D, Maniatis T, Harrison SC, EMBO J. 2004 Nov 10;23(22):4384-93. Epub 2004 Oct 28. PMID:15510218

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