The N-terminal domain of NCOA4 is predicted to form a homodimer. (A) An HHpred search showed that the N-terminal domain of NCOA4 is similar to the coiled-coil domain (residues 244–405) of TRIM28, which forms a homodimer. The coiled-coil domains of TRIM28 (green and gray) are shown (PDB accession no. 6QAJ). (B) The structure of the N-terminal domain (residues 1–182) of NCOA4 (green and gray) is predicted by AlphaFold-Multimer. The putative self-interaction sites Ile-56 (magenta) and Leu-63 (red) are shown. (C) Yeast AH109 cells were transformed with plasmids expressing the N-terminal domain (residues 1–182) of NCOA4 with or without I56E or L63R mutation fused with a transcription activation domain (AD) or a DNA-binding domain (BD). The cells were grown on SD (-Leu, -Trp) or SD (-Leu, -Trp, -Ade) plates.