Extended Data Fig. 6: Inner face key residues at the potential extracellular binding site. | Nature

Extended Data Fig. 6: Inner face key residues at the potential extracellular binding site.

From: Structures of Ostα/β reveal a unique fold and bile acid transport mechanism

Extended Data Fig. 6: Inner face key residues at the potential extracellular binding site.

a Hydrophilic surface of inner lateral lobe. b Hydrophilic surface of inner main lobe. Effects of mutants at the inner cavity on Ostα/β transport activity. c, d Ligands interaction with Ostα/β near the extracellular side. LigPlot+ analysis for cholesterol (blue, c) and DHEAS (green, d). Hydrogen bonds were defined using a donor–acceptor distance cutoff of 3.9 Å, and hydrophobic (non-bonded) contacts were identified within a 2.2–3.9 Å range. e MD simulation distance traces from Ostα/βDHEAS tetramer structure: Lig–G279 (DHEAS sulfur–G279 Cα), Lig–K191 (DHEAS sulfur–K191 side chain nitrogen), P209–E116 (minimum distance), and Lig–palm (minimum distance DHEAS sulfur-7 palmitoylated cysteines).

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