NDLI: Structural basis of DNA recognition by the heterodimeric cell cycle transcription factor E2F

Content Provider	PubMed Central
Author	Zheng, Ning Fraenkel, Ernest Pabo, Carl O. Pavletich, Nikola P.
Copyright Year	1999
Abstract	The E2F and DP protein families form heterodimeric transcriptionfactors that play a central role in the expression of cellcycle-regulated genes. The crystal structure of an E2F4–DP2–DNAcomplex shows that the DNA-binding domains of the E2F and DP proteinsboth have a fold related to the winged-helix DNA-binding motif.Recognition of the central c/gGCGCg/csequence of the consensus DNA-binding site is symmetric, and aminoacids that contact these bases are conserved among all known E2F and DPproteins. The asymmetry in the extended binding siteTTTc/gGCGCc/g is associated with anamino-terminal extension of E2F4, in which an arginine binds in theminor groove near the TTT stretch. This arginine is invariant amongE2Fs but not present in DPs. E2F4 and DP2 interact through an extensiveprotein–protein interface, and structural features of this interfacesuggest it contributes to the preference for heterodimers overhomodimers in DNA binding.
Starting Page	666
File Format	PDF
ISSN	15495477
e-ISSN	15495477
Journal	Genes & Development
Issue Number	6
Volume Number	13
Language	English
Publisher	Cold Spring Harbor Laboratory Press
Publisher Date	1999-03-15
Access Restriction	Open
Rights Holder	Cold Spring Harbor Laboratory Press
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Genetics Developmental Biology

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Structural basis of DNA recognition by the heterodimeric cell cycle transcription factor E2F–DP