1BFS

STRUCTURE OF NF-KB P50 HOMODIMER BOUND TO A KB SITE

Summary for 1BFS

• Entry DOI: 10.2210/pdb1bfs/pdb
• Descriptor: NUCLEAR FACTOR NF-KAPPA-B P50 (2 entities in total)
• Functional Keywords: transcription factor, nf-kb, dimerization domain
• Biological source: Mus musculus (house mouse)
• Cellular location: Nucleus. Isoform 5: Cytoplasm. Isoform 6: Nucleus. Isoform 7: Nucleus: P25799
• Total number of polymer chains: 1
• Total formula weight: 12256.83

Authors

Huang, D.B.,Huxford, T.,Chen, Y.Q.,Ghosh, G. (deposition date: 1997-09-12, release date: 1998-01-28, Last modification date: 2024-02-07)

Primary citation

Huang, D.B.,Huxford, T.,Chen, Y.Q.,Ghosh, G.
The role of DNA in the mechanism of NFkappaB dimer formation: crystal structures of the dimerization domains of the p50 and p65 subunits.
Structure, 5:1427-1436, 1997

PubMed Abstract: Members of the rel/NFkappaB family of transcription factors play a vital role in the regulation of rapid cellular responses, such as those required to fight infection or react to cellular stress. Members of this family of proteins form homo- and heterodimers with differing affinities for dimerization. They share a structural motif known as the rel homology region (RHR), the C-terminal one third of which mediates protein dimerization. Crystal structures of the rel/NFkappaB family members p50 and p65 in their DNA-bound homodimeric form have been solved. These structures showed that the residues from the dimerization domains of both p50 and p65 participate in DNA binding and that the DNA-protein and protein dimerization surfaces form one continuous overlapping interface. We desired to investigate the contribution of DNA to NFkappaB dimerization and to identify the mechanism for the selective association of rel/NFkappaB family peptides into transcriptionally active dimers.

PubMed: 9384558
DOI: 10.1016/S0969-2126(97)00293-1

Experimental method

X-RAY DIFFRACTION (2.2 Å)