2V2T

X-ray structure of a NF-kB p50-RelB-DNA complex

Summary for 2V2T

• Entry DOI: 10.2210/pdb2v2t/pdb
• Related: 1BFS 1IKN 1LE5 1LE9 1LEI 1NFK 1OOA 1U36 1U3J 1U3Y 1U3Z 1U41 1U42 1VKX 1ZK9 1ZKA
• Descriptor: TRANSCRIPTION FACTOR RELB, NUCLEAR FACTOR NF-KAPPA-B P105 SUBUNIT, 5'-D(*CP*GP*GP*GP*AP*AP*TP*TP*CP*CP*CP)-3', ... (4 entities in total)
• Functional Keywords: 4-diphosphocytidyl-2c-methyl-d-erythritol, aquifex aeolicus, nucleotide-binding, isoprene biosynthesis, transcription, kinase, transferase, atp-binding, non-mevalonate
• Biological source: MUS MUSCULUS (MOUSE); More
• Cellular location: Nucleus: Q04863; Nucleus. Isoform 5: Cytoplasm. Isoform 6: Nucleus. Isoform 7: Nucleus: P25799
• Total number of polymer chains: 4
• Total formula weight: 75985.44

Authors

Moorthy, A.K.,Huang, D.B.,Wang, V.Y.,Vu, D.,Ghosh, G. (deposition date: 2007-06-07, release date: 2007-07-03, Last modification date: 2024-11-06)

Primary citation

Moorthy, A.K.,Huang, D.B.,Wang, V.Y.,Vu, D.,Ghosh, G.
X-Ray Structure of a NF-kappaB p50/Relb/DNA Complex Reveals Assembly of Multiple Dimers on Tandem kappaB Sites.
J.Mol.Biol., 373:723-, 2007

PubMed Abstract: 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.

PubMed: 17869269
DOI: 10.1016/J.JMB.2007.08.039

Experimental method

X-RAY DIFFRACTION (3.05 Å)