Figure 1.
Intramolecular interaction in eIF2α. (A) TROSY-HSQC spectra of 2H/15N-labeled eIF2α (black), eIF2α-NTD (blue), and 2H/15N/13C-labeled eIF2α-CTD (red). (B) Boxed area in (A). The arrows indicate movement of peaks away from their full length WT positions. (C) Plot of chemical shift perturbations (CSP) between eIF2α and its individual domains. Gray bars represent indeterminate residues for which no analysis could be performed. Key structural features are shown above the plot for reference, with the extreme end (aa 302–314) of the C-terminal tail (CTT) shown as a wavy line. (D) Residues affected by the intramolecular interaction mapped onto the structure of eIF2α, colored from yellow (>1 standard deviation (σ)) to red (>3σ). Indeterminate residues are colored gray. Residues <1σ are colored black. Residues 302–314 were absent in the NMR structure and are thus not displayed here. (E) Model for the closed conformation of eIF2α shown in ribbon and colored as in panel D.