Structural highlights
Function
[A0A3Q0KSG2_SCHMA] Reversible hydration of carbon dioxide.[RuleBase:RU367011]
Publication Abstract from PubMed
Tegumental carbonic anhydrase from the worm Schistosoma mansoni (SmCA) is considered a new anti-parasitic target because suppressing its expression interferes with schistosome metabolism and virulence. Here, we present the inhibition profiles of selenoureido compounds on recombinant SmCA and resolution of the first X-ray crystal structures of SmCA in adduct with a selection of such inhibitors. The key molecular features of such compounds in adduct with SmCA were obtained and compared to the human isoform hCA II, in order to understand the main structural factors responsible for enzymatic affinity and selectivity. Compounds that more specifically inhibited the schistosome versus human enzymes were identified. The results expand current knowledge in the field and pave the way for the development of more potent antiparasitic agents in the near future.
Structural Insights into Schistosoma mansoni Carbonic Anhydrase (SmCA) Inhibition by Selenoureido-Substituted Benzenesulfonamides.,Angeli A, Ferraroni M, Da'dara AA, Selleri S, Pinteala M, Carta F, Skelly PJ, Supuran CT J Med Chem. 2021 Jul 22;64(14):10418-10428. doi: 10.1021/acs.jmedchem.1c00840., Epub 2021 Jul 7. PMID:34232641[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Angeli A, Ferraroni M, Da'dara AA, Selleri S, Pinteala M, Carta F, Skelly PJ, Supuran CT. Structural Insights into Schistosoma mansoni Carbonic Anhydrase (SmCA) Inhibition by Selenoureido-Substituted Benzenesulfonamides. J Med Chem. 2021 Jul 22;64(14):10418-10428. doi: 10.1021/acs.jmedchem.1c00840., Epub 2021 Jul 7. PMID:34232641 doi:http://dx.doi.org/10.1021/acs.jmedchem.1c00840
