7A6V

Human Carbonic Anhydrase II in complex with 4-(3-(3-phenoxypropyl)thioureido)benzenesulfonamide

Summary for 7A6V

• Entry DOI: 10.2210/pdb7a6v/pdb
• Descriptor: Carbonic anhydrase 2, ZINC ION, GLYCEROL, ... (5 entities in total)
• Functional Keywords: carbonic anhydrase, lyase
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 1
• Total formula weight: 29593.76

Authors

Angeli, A.,Ferraroni, M. (deposition date: 2020-08-26, release date: 2021-10-06, Last modification date: 2024-01-31)

Primary citation

Sbravati, D.,Bonardi, A.,Bua, S.,Angeli, A.,Ferraroni, M.,Nocentini, A.,Casnati, A.,Gratteri, P.,Sansone, F.,Supuran, C.T.
Calixarenes Incorporating Sulfonamide Moieties: Versatile Ligands for Carbonic Anhydrases Inhibition.
Chemistry, 28:e202103527-e202103527, 2022

PubMed Abstract: Carbonic anhydrases (CAs) continue to represent a relevant pharmaceutical target. The need of selective inhibitors and the involvement of these metalloenzymes in many multifaceted diseases boost the search for new ligands able to distinguish among the different CA isoforms, and for multifunctional systems simultaneously able to inhibit CAs and to interfere with other pathological events by interacting with additional targets. In this work, we successfully explored the possibility of preparing new CAs ligands by combining calixarenes with benzensulfonamide units. Inhibition tests towards three human CA isoforms evidenced, for some of the ligands, K values in the nanomolar range and promising selectivity. X-ray and molecular modeling studies provided information on the mode of binding of these calixarene derivatives. Thanks to the encouraging results and the structural features typical of the calixarene scaffold, it is then possible to plan for the future the design of multifunctional inhibitors for this class of widely spread enzymes.

PubMed: 34882858
DOI: 10.1002/chem.202103527

Experimental method

X-RAY DIFFRACTION (2 Å)