Diagram of RPS29 conserved domains and genomic structure. (A) Comparison of amino acid conservation of RPS29 homologs; a higher percent identity at a given position is indicated by a deeper blue color, and the 2 sites of mutation are indicated by the boxes. (B) The three-dimensional model of human 40S RPs³⁵  and RPS29 (UniProt P62273, RS29_HUMAN) was constructed using the UCSF Chimera package.³⁴  Secondary structural domains are shown as ribbons (α-helix; arrow is β-sheet, and tubes are loop regions), and the amino acid side chains of the RPS29 protein are illustrated. The sites of the amino acid substitutions are shown and highlighted in red. (C) Schematic of RPS29 secondary structure (black regions are coils, the green region is a helix, and blue regions are strands) with the sites of the amino acid substitutions shown.