1le9: Difference between revisions

Revision as of 13:17, 2 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1le9.png

Template:STRUCTURE 1le9

Crystal structure of a NF-kB heterodimer bound to the Ig/HIV-kB sitiCrystal structure of a NF-kB heterodimer bound to the Ig/HIV-kB siti

Template:ABSTRACT PUBMED 11970948

About this StructureAbout this Structure

1LE9 is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

The x-ray crystal structure of the NF-kappa B p50.p65 heterodimer bound to the interferon beta -kappa B site., Berkowitz B, Huang DB, Chen-Park FE, Sigler PB, Ghosh G, J Biol Chem. 2002 Jul 5;277(27):24694-700. Epub 2002 Apr 22. PMID:11970948

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Crystal structure of a NF-kB heterodimer bound to the Ig/HIV-kB siti'''
+===Crystal structure of a NF-kB heterodimer bound to the Ig/HIV-kB siti===
-==Overview==
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-We have determined the x-ray crystal structure of the transcription factor NF-kappaB p50.p65 heterodimer complexed to kappaB DNA from the cytokine interferon beta enhancer (IFNbeta-kappaB). To better understand how the binding modes of NF-kappaB on its two best studied DNA targets might contribute to promoter-specific transcription, this structure is compared with the previously determined complex crystal structure containing NF-kappaB bound to the Ig kappa light chain gene enhancer as well as to a second NF-kappaB.Ig kappa light chain gene enhancer complex also reported in this paper. The global binding modes of all NF-kappaB.DNA complex structures are similar, although crystal-packing interactions lead to differences between identical complexes of the same crystallographic asymmetric unit. An extensive network of stacked amino acid side chains that contribute to base-specific DNA contacts is conserved among the three complexes. Consistent with earlier reports, however, the IFNbeta-kappaB DNA is bent significantly less by NF-kappaB than is the Ig kappa light chain gene enhancer. This and other small structural changes may play a role in explaining why NF-kappaB-directed transcription is sensitive to the context of specific promoters. The precise molecular mechanism behind the involvement of the high mobility group protein I(Y) in interferon beta enhanceosome formation remains elusive.
+The line below this paragraph, {{ABSTRACT_PUBMED_11970948}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_11970948}}
 ==About this Structure==
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 [[Category: Nf-kb/dna complex]]
 [[Category: Transcription factor]]
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