NDLI: Structural basis for the recognition of the E2F transactivation domain by the retinoblastoma tumor suppressor

Content Provider	PubMed Central
Author	Lee, Changwook Chang, Jeong Ho Lee, Hyun Sook Cho, Yunje
Copyright Year	2002
Abstract	Repression of E2F transcription activity by the retinoblastoma (Rb) tumor suppressor through its interaction with the transactivation domain of the E2F transcription factor is one of the central features of G1/S arrest in the mammalian cell cycle. Deregulation of the Rb–E2F interaction results in hyperproliferation, lack of differentiation, and apoptosis, and can lead to cancer. The 2.2-Å crystal structure of the Rb pocket complexed with an 18-residue transactivation-domain peptide of E2F-2 reveals that the boomerang-shaped peptide binds to the highly conserved interface between the A-box and the B-box of the Rb pocket in a bipartite manner. The N-terminal segment of the E2F-2 peptide in an extended β-strand-like structure interacts with helices from the conserved groove at the A–B interface, whereas the C-terminal segment, which contains one 310 helix, binds to a groove mainly formed by A-box helices. The flexibility in the middle of the E2F-2 peptide is essential for the tight association of E2F to the Rb pocket. The binding of Rb to the E2F-2 peptide conceals several conserved residues that are crucial for transcription activation of E2F. We provide the structural basis for the Rb-mediated repression of E2F transcription activity without the requirement of histone-modifying enzymes.
Related Links	http://dx.doi.org/10.1101/gad.1046102
Ending Page	3212
Page Count	14
Starting Page	3199
File Format	PDF
ISSN	08909369
Journal	Genes & Development
Issue Number	24
Volume Number	16
Language	English
Publisher	Cold Spring Harbor Laboratory Press
Publisher Date	2002-12-15
Access Restriction	Open
Rights Holder	Cold Spring Harbor Laboratory Press
Subject Keyword	Medicine(all) Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Genetics Developmental Biology

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