2RAM

A NOVEL DNA RECOGNITION MODE BY NF-KB P65 HOMODIMER

2RAM の概要

• エントリーDOI: 10.2210/pdb2ram/pdb
• 分子名称: DNA (5'-D(*CP*GP*GP*CP*TP*GP*GP*AP*AP*AP*TP*(5IU)P*(5IU)P*CP*CP*AP*GP*CP*CP*G)-3'), PROTEIN (TRANSCRIPTION FACTOR NF-KB P65), (2S,3S)-1,4-DIMERCAPTOBUTANE-2,3-DIOL, ... (4 entities in total)
• 機能のキーワード: complex (transcription factor-dna), dna-binding, transcription regulation, activator nuclear protein, phosphorylation, conformation, transcription-dna complex, transcription/dna
• 由来する生物種: Mus musculus (house mouse)
• 細胞内の位置: Nucleus: Q04207
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 75046.07

構造登録者

Chen, Y.Q.,Ghosh, S.,Ghosh, G. (登録日: 1997-11-23, 公開日: 1998-05-27, 最終更新日: 2024-02-21)

主引用文献

Chen, Y.Q.,Ghosh, S.,Ghosh, G.
A novel DNA recognition mode by the NF-kappa B p65 homodimer.
Nat.Struct.Biol., 5:67-73, 1998

PubMed Abstract: The crystal structure of the NF-kappa B p65 (RelA) homodimer in complex with a DNA target has been determined to 2.4 A resolution. The two p65 subunits are not symmetrically disposed on the DNA target. The homodimer should optimally bind to a pseudo-palindromic nine base pair target with each subunit recognizing a 5'GGAA-3' half site separated by a central A-T base pair. However, one of the subunits (subunit B) encounters a half site of 5'-GAAA-3'. The single base-pair change from G-C to A-T results in highly unfavorable interactions between this half site and the base contacting protein residues in subunit B, which leads to an 18 degrees rotation of the N-terminal terminal domain from its normal conformation. Remarkably, subunit B retains all the interactions with the sugar phosphate backbone of the DNA target. This mode of interaction allows the NF-kappa B p65 homodimer to recognize DNA targets containing only one cognate half site. Differences in the sequence of the other half site provide variations in conformation and affinity of the complex.

PubMed: 9437432
DOI: 10.1038/nsb0198-67

実験手法

X-RAY DIFFRACTION (2.4 Å)