HIGHLIGHTS
SUMMARY
Positive controls were docked into the binding_sites of SERCA2b, Slo1, and the SUR2 subunit of KATP, as a means to validate the docking procedure. One carboxyl moiety was also involved in hydrogen_bonding with Thr744 and formed a carbon hydrogen_bond with Glu742. The studied asymmetric porphyrin derivatives were docked on a binding pocket of SERCA2b that overlaps with the BHQ binding_site. The docking results indicate that both the free base porphyrin derivative and its corresponding metalloporphyrins have the potential to inhibit SERCA2b by interacting with the same binding_site. The same observation could be made for . . .
If you want to have access to all the content you need to log in!
Thanks :)
If you don't have an account, you can create one here.