Fig. 2.
Superposition of the C-DENR110–195 structure (coral) with: A. the structure of the human C-DENR (light gray) bound to the human 40S subunit; B. the NMR structure of the human eIF1 (green, PDB: 2IF1, amino acid residues 28–108); C. the structure of the human C-eIF2D (gray, PDB: 5W2F); D. structures of archaeal aIF1 (blue, PDB: 5ZCY) and bacterial YciH (yellow, PDB: 1D1R). The basic loop and β-hairpin 2 loop are marked by an arrow; N- and C-terminus of a protein are marked by N and C, respectively. Positions of amino acid residues of C-DENR are presented by spheres: Pro121 (red), Lys125 (gold), Cys154 (blue). A crosslink between residues Lys125 and Cys154 is marked by a dotted line. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)