2v2t: Difference between revisions

Revision as of 01:00, 29 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:2v2t.png

Template:STRUCTURE 2v2t

X-RAY STRUCTURE OF A NF-KB P50-RELB-DNA COMPLEXX-RAY STRUCTURE OF A NF-KB P50-RELB-DNA COMPLEX

Template:ABSTRACT PUBMED 17869269

About this StructureAbout this Structure

2V2T is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

X-ray structure of a NF-kappaB p50/RelB/DNA complex reveals assembly of multiple dimers on tandem kappaB sites., Moorthy AK, Huang DB, Wang VY, Vu D, Ghosh G, J Mol Biol. 2007 Oct 26;373(3):723-34. Epub 2007 Aug 22. PMID:17869269

Page seeded by OCA on Tue Jul 29 01:00:23 2008

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

OCA

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-'''X-RAY STRUCTURE OF A NF-KB P50-RELB-DNA COMPLEX'''
+===X-RAY STRUCTURE OF A NF-KB P50-RELB-DNA COMPLEX===
-==Overview==
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-We describe here the X-ray crystal structure of NF-kappaB p50/RelB heterodimer bound to a kappaB DNA. Although the global modes of subunit association and kappaB DNA recognition are similar to other NF-kappaB/DNA complexes, this complex reveals distinctive features not observed for non-RelB complexes. For example, Lys274 of RelB is removed from the protein-DNA interface whereas the corresponding residues in all other subunits make base-specific contacts. This mode of binding suggests that RelB may allow the recognition of more diverse kappaB sequences. Complementary surfaces on RelB and p50, as revealed by the crystal contacts, are highly suggestive of assembly of multiple p50/RelB heterodimers on tandem kappaB sites in solution. Consistent with this model our in vitro binding experiments reveal optimal assembly of two wild-type p50/RelB heterodimers on tandem HIV kappaB DNA with 2 bp spacing but not by a mutant heterodimer where one of the RelB packing surface is altered. We suggest that multiple NF-kappaB dimers assemble at diverse kappaB promoters through direct interactions utilizing unique protein-protein interaction surfaces.
+The line below this paragraph, {{ABSTRACT_PUBMED_17869269}}, adds the Publication Abstract to the page
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