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. Author manuscript; available in PMC: 2016 Mar 29.
Published in final edited form as: Nat Struct Mol Biol. 2013 May 5;20(6):735–739. doi: 10.1038/nsmb.2572

Figure 3.

Figure 3

Analysis of TTP–CNOT1 interaction. (A) Electron density (grey) of the TTP312–326 peptide (shown as purple sticks). Density (Fo-Fc of a map calculated by omitting the TTP peptide) is contoured at 2.5σ. (B) A view of the interface between the CNOT1 domain (grey) and TTP peptide (purple). Interacting side chains of CNOT1 (blue) and TTP (purple) are shown as sticks. The backbone amide of P317 is shown as a blue sphere. Dashed lines indicate hydrogen-bonding interactions. (C) Recombinant glutathione-S-transferase (GST)–tagged CNOT1800–1015 (Figure 1B) was immobilized on glutathione-Sepharose beads and incubated with (MBP)–tagged TTP-CTD, or TTP-CTD mutants. Precipitated proteins were separated by SDS-PAGE and visualized by Coomassie staining.