Fig. 2: Dimer interface of hSMPD2.
From: Molecular basis for the catalytic mechanism of human neutral sphingomyelinases 1 (hSMPD2)
a Ribbon representation of hSMPD2 with one protomer shown in cylinder and the other protomer shown in surface electrostatics. b Hydrophobic interactions between the TM regions of hSMPD2. The four lipids are colored blue. c Magnification of the polar interactions between different monomers of hSMPD2 from the bottom view. d In vitro pull-down assays of the hSMPD2 mutants by using the Strep tagged hSMPD2 as a bait protein. Source data are provided as a Source Data file. e Multiple unbiased MD simulations after the equilibration phase indicates a stable salt bridge that formed by E92 and K168 throughout the MD simulations. f Relative enzyme activity of wild type hSMPD2 and the indicated dimer interface-related mutants; mean ± SEM, n = 4 biological replicates. Source data are provided as a Source Data file.
