Fig. 2: Specific interactions around the entry channel mediate the binding of Pdcd4-NTD to the 40S. | Nature Communications

Fig. 2: Specific interactions around the entry channel mediate the binding of Pdcd4-NTD to the 40S.

From: Human tumor suppressor protein Pdcd4 binds at the mRNA entry channel in the 40S small ribosomal subunit

Fig. 2

A Pdcd4-NTD binds to the ribosomal protein uS3. B W124 in Pdcd4-NTD is anchored to a hydrophobic pocket in uS3, and plays a critical role in this interaction. C K114 and K115 in Pdcd4-NTD also makes specific interactions with h18 in 18S rRNA. D Fluorescence anisotropy competition assay using labeled Pdcd4-NTD similar to Fig. 1B, showing that residues described in B and C are critical for the binding of Pdcd4 to the 40S. V123A/W124A and K114A/K115A mutants almost completely lose their affinity for the 40S, which is comparable to deletion of the entire NTD (Pdcd4-CTD, residues 157-469). Error bars represent the mean ± SEM (n = 3). For the NTD, only two independent experiments were performed. The experiment was repeated at least three times with similar results.

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