Structural Conservation and E2F Binding Specificity within the Retinoblastoma Pocket Protein Family
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- 作者：Tyler J. Liban1 ; Michael J. Thwaites2 ; Frederick A. Dick2 ; Seth M. Rubin1 ; srubin@ucsc.edu" class="auth_mail" title="E-mail the corresponding author
- 关键词：Rb ; retinoblastoma ; Cdk ; Cyclin-dependent kinase ; E2FTD ; E2F transactivation domain ; p107/p130 ; p107 or p130 ; RbN ; Rb containing a structured N-terminal domain ; RbC ; Rb containing an intrinsically disordered C-terminal domain ; RbPL ; Rb containing a ; ~ ; 60 aa loop in the pocket domain ; p107N ; p107 has a predicted structured N-terminal domain ; p107PL ; loop within p107 pocket domain ; ITC ; isothermal titration calorimetry ; p1076x-FL ; six E2F-binding mutations into full-length p107 ; GST ; glut
- 刊名：Journal of Molecular Biology
- 出版年：2016
- 出版时间：9 October 2016
- 年：2016
- 卷：428
- 期：20
- 页码：3960-3971
- 全文大小：1881 K
文摘
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Pocket proteins (Rb, p107, and p130) and E2F transcription factors regulate cell-cycle-dependent gene expression.
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Specific interactions between these proteins are due to affinity differences between the E2F transactivation domain and the pocket domain.
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Mutating key interacting residues in the pocket domain of p107 results in a protein that binds E2F2-like Rb and regulates its transcription activity in cells.
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Although phosphorylation of p107 is inefficient in vitro compared to Rb, analogous modifications inhibit E2F binding.