Summary information and primary citation
- PDB-id
-
1cf7;
DSSR-derived features in text and
JSON formats; DNAproDB
- Class
- transcription-DNA
- Method
- X-ray (2.6 Å)
- Summary
- Structural basis of DNA recognition by the
heterodimeric cell cycle transcription factor e2f-dp
- Reference
-
Zheng N, Fraenkel E, Pabo CO, Pavletich NP (1999):
"Structural
basis of DNA recognition by the heterodimeric cell cycle
transcription factor E2F-DP." Genes Dev.,
13, 666-674.
- 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.
