Fig 1: The characterization and computational simulation of MOP-1.A The photo of MOP-1 aqueous solution (left). Monodisperse structure of MOP-1 in H2O (right). Color codes: V, green; O, red; C, gray; N, blue; Cl, bright blue. The large pink sphere represents the free space inside the molecular cage. For clarity, H atoms were omitted. Schematic (right panel) was created with Diamond software. B Experimental and simulated PXRD patterns of MOP-1. C TEM image of MOP-1 (left). Scale bar, 20 nm. The particle size of MOP-1 in H2O (right). Three experiments were repeated independently with similar results. D The schematic diagram showed that the SHP-2 mediated STAT3 inactivation. Schematic diagram was created with Microsoft Office PowerPoint. E, F An in-depth mechanism investigation of mESC pluripotency control by MOP-1. Binding model from a global view of a complex composed of SHP-2 and MOP-1 illustrated by electrostatic surface potential (E). Binding modes are illustrated by ribbon diagrams of a complex composed of SHP-2 and MOP-1 (the left panel), a complex composed of SHP-2 with MOP (the middle panel) and a complex composed of SHP-2 with ZrMOP (the right panel). The top panel is the global view of the catalytic PTP structure of SHP-2, the bottom panel is the focused view of binding modes illustrated by the Ribbon diagrams (F). G Binding kinetics of MOP-1 (top panel) and MOP-2 (bottom panel) with SHP-2 were measured by the SPR assay. H The ICP-MS analysis of the binding quantity between MOPs and SHP-2 (mean ± s.e.m, n = 6). I The inhibition efficiency of SHP-2, JAK2, JAK1, SHP-1, PTP1B, Cyt c, ACP and lipase by MOP-1 at a concentration of 2 μM using enzyme assay (mean ± s.e.m, n = 3). Data in (H) and (I) are analyzed by one-way ANOVA. ****P < 0.0001, the binding between MOP-1 and SHP-2 vs. the binding between MOP-2 and SHP-2, relative activity of SHP-2 vs. relative activity of JAK2, JAK1, PTP1B, Cyt c, ACP and lipase. ***P < 0.001, relative activity of SHP-2 vs. relative activity of SHP-1.