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 2.80Å" /> '''Structure of NF-kB p...)
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Revision as of 10:04, 21 November 2007
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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
Page seeded by OCA on Wed Nov 21 12:12:05 2007
