2i9t

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(New page: 200px<br /><applet load="2i9t" size="450" color="white" frame="true" align="right" spinBox="true" caption="2i9t, resolution 2.80&Aring;" /> '''Structure of NF-kB p...)
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[[Image:2i9t.gif|left|200px]]<br /><applet load="2i9t" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2i9t, resolution 2.80&Aring;" />
caption="2i9t, resolution 2.80&Aring;" />
'''Structure of NF-kB p65-p50 heterodimer bound to PRDII element of B-interferon promoter'''<br />
'''Structure of NF-kB p65-p50 heterodimer bound to PRDII element of B-interferon promoter'''<br />
==Overview==
==Overview==
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Upon viral infection, NF-kappaB translocates to the nucleus and activates, the IFN-beta gene by binding to the PRDII element. Strikingly, NF-kappaB, loses its ability to activate the IFN-beta gene when the PRDII element is, substituted by closely related sites. We report here the crystal structure, of NF-kappaB p50/p65 heterodimer bound to the PRDII element from the, IFN-beta promoter. The structure reveals an unexpected alteration in, configuration, in which the p50 specificity domain moves by as much as, approximately 9 A when compared to NF-kappaB heterodimer bound to the, immunoglobulin kappaB site (Ig-kappaB) while maintaining the same, base-specific contacts with the DNA. Taken together, the structure offers, new insights into the allosteric effects of closely related DNA sites on, the configuration of NF-kappaB and its transcriptional selectivity.
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Upon viral infection, NF-kappaB translocates to the nucleus and activates the IFN-beta gene by binding to the PRDII element. Strikingly, NF-kappaB loses its ability to activate the IFN-beta gene when the PRDII element is substituted by closely related sites. We report here the crystal structure of NF-kappaB p50/p65 heterodimer bound to the PRDII element from the IFN-beta promoter. The structure reveals an unexpected alteration in configuration, in which the p50 specificity domain moves by as much as approximately 9 A when compared to NF-kappaB heterodimer bound to the immunoglobulin kappaB site (Ig-kappaB) while maintaining the same base-specific contacts with the DNA. Taken together, the structure offers new insights into the allosteric effects of closely related DNA sites on the configuration of NF-kappaB and its transcriptional selectivity.
==About this Structure==
==About this Structure==
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2I9T is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2I9T OCA].
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2I9T is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=2I9T OCA].
==Reference==
==Reference==
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Aggarwal, A.K.]]
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[[Category: Aggarwal, A K.]]
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[[Category: Escalante, C.R]]
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[[Category: Escalante, C R]]
[[Category: Shen, L.]]
[[Category: Shen, L.]]
[[Category: Thanos, D.]]
[[Category: Thanos, D.]]
[[Category: protein-dna complex]]
[[Category: protein-dna complex]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 12:12:05 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:50:24 2008''

Revision as of 15:50, 21 February 2008


2i9t, resolution 2.80Å

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Structure of NF-kB p65-p50 heterodimer bound to PRDII element of B-interferon promoter

Overview

Upon viral infection, NF-kappaB translocates to the nucleus and activates the IFN-beta gene by binding to the PRDII element. Strikingly, NF-kappaB loses its ability to activate the IFN-beta gene when the PRDII element is substituted by closely related sites. We report here the crystal structure of NF-kappaB p50/p65 heterodimer bound to the PRDII element from the IFN-beta promoter. The structure reveals an unexpected alteration in configuration, in which the p50 specificity domain moves by as much as approximately 9 A when compared to NF-kappaB heterodimer bound to the immunoglobulin kappaB site (Ig-kappaB) while maintaining the same base-specific contacts with the DNA. Taken together, the structure offers new insights into the allosteric effects of closely related DNA sites on the configuration of NF-kappaB and its transcriptional selectivity.

About this Structure

2I9T is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.

Reference

Structure of NF-kappaB p50/p65 heterodimer bound to the PRDII DNA element from the interferon-beta promoter., Escalante CR, Shen L, Thanos D, Aggarwal AK, Structure. 2002 Mar;10(3):383-91. PMID:12005436

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