Fig. 3: Mapping of the μs-ms dynamics of the eIF4G-interacting domains. | Nature Communications

Fig. 3: Mapping of the μs-ms dynamics of the eIF4G-interacting domains.

From: Dynamically regulated two-site interaction of viral RNA to capture host translation initiation factor

Fig. 3

a Left: Residue-specific Rex values of the J domain. The residues that could not be analyzed quantitatively, due to extensive conformational exchanges in the μs-ms time scale, are shown as gray backgrounds. Middle and right: Mapping of the Rex values in the secondary structure (middle) and tertiary structure of the previously reported J domain (right, PDB ID: 2NBY)9. The Ade/Gua residues that exhibited Rex values larger than 10 s−1 are colored red, whereas those between 5 and 10 s−1 are cyan. Source data are provided as a Source Data file. b Left: Residue-specific Rex values of the StASL domain. Residues that could not be analyzed quantitatively, due to extensive conformational exchanges in the μs-ms time scale, are shown with a gray background. Middle and right: Mapping of the Rex values in the secondary structure (middle) and tertiary structure model (right), which is derived from the previously reported structure of the ΔJΔK domain9 (PDB ID: 2NC1) by substituting the GAAA tetraloops with the UUCG tetraloops. The Ade/Gua residues that exhibited Rex values larger than 10 s−1 are colored red, whereas those between 5 and 10 s−1 are cyan. Source data are provided as a Source Data file. Error bars indicate experimental errors derived from the signal-to-noise ratio of each correlation, as written in Methods.

Back to article page