9H0Q
N terminal domain of BC2L-C lectin in complex with N-(beta-L-Fucopyranosyl)-biphenyl-3-carboxamide
Summary for 9H0Q
| Entry DOI | 10.2210/pdb9h0q/pdb |
| Related | 9G3K 9G3L |
| Descriptor | Lectin, N-(beta-L-Fucopyranosyl)-biphenyl-3-carboxamide, TETRAETHYLENE GLYCOL, ... (5 entities in total) |
| Functional Keywords | lectin, beta-fucosylamide, burkholderia, anti-adhesive, sugar binding protein |
| Biological source | Burkholderia cenocepacia J2315 |
| Total number of polymer chains | 10 |
| Total formula weight | 145140.96 |
| Authors | Antonini, G.,Varrot, A. (deposition date: 2024-10-08, release date: 2025-04-16, Last modification date: 2025-05-21) |
| Primary citation | Antonini, G.,Fares, M.,Hauck, D.,Mala, P.,Gillon, E.,Belvisi, L.,Bernardi, A.,Titz, A.,Varrot, A.,Mazzotta, S. Toward Dual-Target Glycomimetics against Two Bacterial Lectins to Fight Pseudomonas aeruginosa - Burkholderia cenocepacia Infections: A Biophysical Study. J.Med.Chem., 68:9681-9693, 2025 Cited by PubMed Abstract: Chronic lung infections caused by and pose a severe threat to immunocompromised patients, particularly those with cystic fibrosis. These pathogens often infect the respiratory tract, and available treatments are limited due to antibiotic resistance. Targeting bacterial lectins involved in biofilm formation and host-pathogen interactions represents a promising therapeutic strategy. In this study, we evaluate the potential of synthetic fucosylamides as inhibitors of the two lectins LecB () and BC2L-C-Nt (). Using a suite of biophysical assays, we assessed their binding affinities, identifying three β-fucosylamides as promising dual-target ligands, while crystallography studies revealed the atomic basis of these ligands to interact with both bacterial lectins. The emerged classes of compounds represent a solid starting point for the necessary hit-to-lead optimization for future dual inhibitors aiming at the treatment of coinfections with these two bacterial pathogens. PubMed: 40279549DOI: 10.1021/acs.jmedchem.5c00405 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.55 Å) |
Structure validation
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