Fig. 5: The three-dimensional structure of the APC homodimer.
From: Predicting colorectal cancer risk in FAP patients using patient-specific organoids
A Schematic primary structure of the resulting truncated APC forms characterizing FAP1, FAP2 and FAP3-hESC lines. The APC regions binding target proteins are indicated below. B The full APC-APC homodimer. a APC 1-730: APC 1-730 homodimer aligned on residues 1–85 where the mutation of FAP3 is located. b The two monomers are shown in green and light blue (left); The AlphaFold results show high model confident (right). c The homodimer structure is held is shape by either intermolecular salt bridge (left; Gln12 & Lys17; or Glu19 & Arg 24), and/or intermolecular hydrogen bonds (right; Ala4-Tyr6-Leu9; Leu10-Gln12; Val13-Leu16; Lys17-Asn20; Leu23-Arg24; Leu27-Asn30; His33-Leu34; Leu37-Leu48; Gln65-Leu72). C, a APC 1-730: APC 1-730 homodimer aligned on residues 5-57 where the mutation of FAP3 is located. b The two monomers are shown in green and light blue (left); The AlphaFold results show high model confident (right). c The homodimer structure is held is shaped by either intermolecular salt bridge (left; Glu20 & Arg26) and/or intermolecular contacts involving the indicated residues (right; Leu9-Leu10-Gln12; Val13-Leu16; Glu19-Asn20; Leu23-Arg24; Leu27-Asn30; His33-Leu34-Leu48).
