1vkx
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CRYSTAL STRUCTURE OF THE NFKB P50/P65 HETERODIMER COMPLEXED TO THE IMMUNOGLOBULIN KB DNA
OverviewOverview
The NF-kappaB p50/p65 heterodimer is the classical member of the Rel, family of transcription factors which regulate diverse cellular functions, such as immune response, cell growth, and development. Other mammalian Rel, family members, including the proteins p52, proto-oncoprotein c-Rel, and, RelB, all have amino-terminal Rel-homology regions (RHRs). The RHR is, responsible for the dimerization, DNA binding and cytosolic localization, of these proteins by virtue of complex formation with inhibitor kappaB, proteins. Signal-induced removal of kappaB inhibitors allows translocation, of dimers to the cell nucleus and transcriptional regulation of kappaB, DNA-containing genes. NF-kappaB specifically recognizes kappaB DNA, elements with a consensus sequence of 5'-GGGRNYYYCC-3' (R is an, unspecified purine; Y is an unspecified pyrimidine; and N is any, nucleotide). Here we report the crystal structure at 2.9 A resolution of, the p50/p65 heterodimer bound to the kappaB DNA of the intronic enhancer, of the immunoglobulin light-chain gene. Our structure reveals a, 5-base-pair 5' subsite for p50, and a 4-base-pair 3' subsite for p65. This, structure indicates why the p50/p65 heterodimer interface is stronger than, that of either homodimer. A comparison of this structure with those of, other Rel dimers reveals that both subunits adopt variable conformations, in a DNA-sequence-dependent manner. Our results explain the different, behaviour of the p50/p65 heterodimer with heterologous promoters.
About this StructureAbout this Structure
1VKX is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of p50/p65 heterodimer of transcription factor NF-kappaB bound to DNA., Chen FE, Huang DB, Chen YQ, Ghosh G, Nature. 1998 Jan 22;391(6665):410-3. PMID:9450761
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