1CF7

STRUCTURAL BASIS OF DNA RECOGNITION BY THE HETERODIMERIC CELL CYCLE TRANSCRIPTION FACTOR E2F-DP

1CF7 の概要

• エントリーDOI: 10.2210/pdb1cf7/pdb
• 分子名称: DNA (5'-D(*AP*TP*TP*TP*TP*CP*GP*CP*GP*CP*GP*GP*TP*TP*TP*T)-3'), DNA (5'-D(*TP*AP*AP*AP*AP*CP*CP*GP*CP*GP*CP*GP*AP*AP*AP*A)-3'), PROTEIN (TRANSCRIPTION FACTOR E2F-4), ... (5 entities in total)
• 機能のキーワード: e2f, dp, winged-helix, dna-binding domain, transcription factor, cell cycle, transcription-dna complex, transcription/dna
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Nucleus: Q16254 Q14188
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 28984.47

構造登録者

Zheng, N.,Fraenkel, E.,Pabo, C.O.,Pavletich, N.P. (登録日: 1999-03-24, 公開日: 1999-04-02, 最終更新日: 2023-12-27)

主引用文献

Zheng, N.,Fraenkel, E.,Pabo, C.O.,Pavletich, N.P.
Structural basis of DNA recognition by the heterodimeric cell cycle transcription factor E2F-DP.
Genes Dev., 13:666-674, 1999

PubMed Abstract: The E2F and DP protein families form heterodimeric transcription factors that play a central role in the expression of cell cycle-regulated genes. The crystal structure of an E2F4-DP2-DNA complex shows that the DNA-binding domains of the E2F and DP proteins both have a fold related to the winged-helix DNA-binding motif. Recognition of the central c/gGCGCg/c sequence of the consensus DNA-binding site is symmetric, and amino acids that contact these bases are conserved among all known E2F and DP proteins. The asymmetry in the extended binding site TTTc/gGCGCc/g is associated with an amino-terminal extension of E2F4, in which an arginine binds in the minor groove near the TTT stretch. This arginine is invariant among E2Fs but not present in DPs. E2F4 and DP2 interact through an extensive protein-protein interface, and structural features of this interface suggest it contributes to the preference for heterodimers over homodimers in DNA binding.

PubMed: 10090723

実験手法

X-RAY DIFFRACTION (2.6 Å)