Structure of the Rb C-terminal domain bound to E2F1-DP1: A mechanism for phosphorylation-induced E2F release
Article Abstract:
A high-affinity interaction between retinoblastoma (Rb) C terminal domain (RbC) and E2F-DP heterodimers shared by all Rb and E2F family members is demonstrated, the crystal structure of an RbC-E2F1-DP1complex shows an intertwined heterodimer in which the marked box domains of both E2F1 and DP1contact RbC. It shows the requirement of RbC for high affinity E2F binding and growth suppression and establishes a mechanism for the regulation of RbE2F association by phosphorylation.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2005
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Structure of DDB1 in complex with a paramyxovirus v protein: Viral hijack of a propeller cluster in ubiquitin ligase
Article Abstract:
The DDB1-Cul4A ubiquitin ligase complex promotes protein ubiquitination in diverse cellular functions and is reprogrammed by the V proteins of paramyxoviruses to degrade STATs and block interferon signaling. The evolutionally conserved DDB1 protein adopts a striking intertwined three-propeller fold, featuring multiple protein binding sites exquisitely organized in space.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2006
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Structure of the Cand1-Cul1-Roc1 complex reveals regulatory mechanisms for the assembly of the multisubunit cullin-dependent ubiquitin ligases
Article Abstract:
Cand1, a 120 kDa HEAT repeat protein, forms a tight complex with the Cul1-Roc1 SCF catalytic core, inhibiting the assembly of the multisubunit E3 complex. An examination of the crystal structure of the Cand1-Cul1-Roc1 tenary complex reveals the detailed mechanisms of how Cand1 participates in regulating the assembly and disassembly of the SCF ubiquitin ligase complex.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2004
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