Multiple LPA₃ Receptor Agonist Binding Sites Evidenced Under Docking and Functional Studies.

ABSTRACT: Comparative studies using lysophosphatidic acid (LPA) and the synthetic agonist, oleoyl-methoxy glycerophosphothionate (OMPT), in cells expressing the LPA₃ receptor revealed differences in the action of these agents. The possibility that more than one recognition cavity might exist for these ligands in the LPA₃ receptor was considered. We performed agonist docking studies exploring the whole protein to obtain tridimensional details of the ligand-receptor interaction. Functional in cellulo experiments using mutants were also executed. Our work includes blind docking using the unrefined and refined proteins subjected to hot spot predictions. Distinct ligand protonation (charge -1 and -2) states were evaluated. One LPA recognition cavity is located near the lower surface

SUBMITTER: Solis KH 

PROVIDER: S-EPMC12071260 | biostudies-literature | 2025 Apr

REPOSITORIES: biostudies-literature