8BOE
Human Carbonic Anhydrase I in complex with (S)-4-(3-(1-(6-nitropyridin-2-yl)pyrrolidin-3-yl)thioureido)benzenesulfonamide
This is a non-PDB format compatible entry.
Summary for 8BOE
| Entry DOI | 10.2210/pdb8boe/pdb |
| Descriptor | Carbonic anhydrase 2, GLYCEROL, ZINC ION, ... (5 entities in total) |
| Functional Keywords | carbonic anhydrase ii, metalloenzyme, inhibitor, sulfonamide, lyase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 29869.05 |
| Authors | Angeli, A.,Ferraroni, M. (deposition date: 2022-11-15, release date: 2023-11-29, Last modification date: 2026-03-04) |
| Primary citation | Angeli, A.,Micheli, L.,Carta, F.,Ferraroni, M.,Pirali, T.,Fernandez Carvajal, A.,Ferrer Montiel, A.,Di Cesare Mannelli, L.,Ghelardini, C.,Supuran, C.T. First-in-Class Dual Hybrid Carbonic Anhydrase Inhibitors and Transient Receptor Potential Vanilloid 1 Agonists Revert Oxaliplatin-Induced Neuropathy. J.Med.Chem., 66:1616-1633, 2023 Cited by PubMed Abstract: Here, we report for the first time a series of compounds potentially useful for the management of oxaliplatin-induced neuropathy (OINP) able to modulate the human Carbonic Anhydrases (hCAs) as well as the Transient Receptor Potential Vanilloid 1 (TRPV1). All compounds showed effective inhibition activity toward the main hCAs involved in such a pathology, whereas selected items reported moderate agonism of TRPV1. X-ray crystallographic experiments assessed the binding modes of the two enantiomers ()- and ()- within the hCA II cleft. Although the tails assumed diverse orientations, no appreciable effects were observed for their hCA II affinity. Similarly, the activity of ()- and ()- on TRPV1 was not influenced by the stereocenters. evaluation of the most promising derivatives ()-, ()-, and the two enantiomers ()-, ()- revealed antihypersensitivity effects in a mouse model of OINP with potent and persistent effect up to 75 min after administration. PubMed: 36626645DOI: 10.1021/acs.jmedchem.2c01911 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.55 Å) |
Structure validation
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