1BFT

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

1BFT の概要

• エントリーDOI: 10.2210/pdb1bft/pdb
• 分子名称: NUCLEAR FACTOR NF-KAPPA-B P65 (2 entities in total)
• 機能のキーワード: transcription factor, nf-kb, dimerization domain
• 由来する生物種: Mus musculus (house mouse)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 22947.87

構造登録者

Huang, D.B.,Huxford, T.,Chen, Y.Q.,Ghosh, G. (登録日: 1997-09-12, 公開日: 1998-01-28, 最終更新日: 2024-04-03)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2 Å)