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Vol. 13, No. 6, pp. 666-674, March 15, 1999
1 Howard Hughes Medical Institute, Cellular Biochemistry
and Biophysics Program, Memorial Sloan-Kettering Cancer Center, New
York, New York 10021 USA; 2 Howard Hughes Medical Institute,
Department of Biology, Massachusetts Institute of Technology,
Cambridge, Massachusetts 02139 USA
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.
[Key Words: E2F; DP; Winged-helix, DNA-binding domain; transcription factor; cell cycle]
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