Fig. 9: CLCC1 homologs are predicted to form oligomers.
From: ER protein CLCC1 promotes nuclear envelope fusion in herpesviral and host processes
a AlphaFold models of the core region of human CLCC1 (residues 161-360, shown schematically at the top) as a hexamer (left), decamer (middle), or hexadecamer (right). Structural elements and domains are colored as in Fig. 6: TM1 (blue), TM2 (deep teal), FD (magenta), AH (orange), and TM3 (teal). b ipTM scores for AlphaFold models of the core region of human CLCC1 (residues 161-360) with number of copies from 2 to 22. c AlphaFold models of the core region of OsHV-1 ORF57 (residues 66-268, shown schematically at the top) as a hexamer (left), decamer (middle), or hexadecamer (right). Structural elements and domains are colored as in (a). d Tilted view of the AlphaFold-generated hexadecameric model of human CLCC1 (residues 161-360) in surface representation. Structural elements and domains are colored as in Fig. 6: TM1 (blue), TM2 (deep teal), FD (pink), AH (orange), and TM3 (teal). FD h2 is shown in magenta. The conserved residue D277 is shown in green. The rest of the residues are shown in wheat. e Cross-section view of the hexadecameric model in (D) in cartoon and semitransparent surface representation. Colors are as in (d). f Up-close view of D277 (green), predicted to form a salt bridge with residue K246 (white) in the adjacent protomer in the model of the human CLCC1 hexadecamer. Colors are as in (d). Source data for graphs are provided in Source Data 9.
