Fig. 2: Cryo-EM structure of hSLC15A4 in complex with Fab107.
From: Development of conformation-selective antibodies targeting human SLC15A4
a Cryo-EM density map of hSLC15A4-Fab107 complex. b Overall structure of Fab107 in complex with hSLC15A4 in luminal-open conformation. NTD and CTD are colored in palegreen and lightblue respectively, bundle bridge is colored in cyan, and light chain and heavy chain of Fab107 are colored in orange and violet respectively in (a, b). c Hydrogen bonding interactions between the endolysosomal lumen loops of hSLC15A4 and the light chain of Fab107. Key residues are shown as sticks and hydrogen bonds are represented as yellow dashed lines. d Hydrogen bonding interactions between the endolysosomal lumen loops of hSLC15A4 and the heavy chain of Fab107. Key residues are shown as sticks and hydrogen bonds are represented as yellow dashed lines. e Hydrophobic interactions between hSLC15A4 and the heavy chain of Fab107. Key residues are shown as sticks and dots. f Flow cytometric analyses showing the binding ability of wild type (WT) hSLC15A4 and its mutants to Ab107. Data are representative of two independent experiments. g CTD-centered structural superimposition of the cytoplasmic-open hSLC15A4 and the luminal-open hSLC15A4-Fab107. Sterically hindered residues are shown as sphere.
