5IDK
Crystal structure of West Nile Virus NS2B-NS3 protease in complex with a capped dipeptide boronate inhibitor
Summary for 5IDK
| Entry DOI | 10.2210/pdb5idk/pdb |
| Descriptor | Genome polyprotein,SERINE PROTEASE SUBUNIT NS2B, SERINE PROTEASE NS3, ((R)-1-((S)-3-(4-(aminomethyl)phenyl)-2-benzamidopropaneamido)-4-guanidinobutyl)boronic acid, cyclic double ester with glycerol, DIMETHYL SULFOXIDE, ... (5 entities in total) |
| Functional Keywords | antivirus agents, peptides, west nile virus, boronic acid, viral protein |
| Biological source | West Nile virus (WNV) More |
| Total number of polymer chains | 3 |
| Total formula weight | 75508.54 |
| Authors | Hilgenfeld, R.,Zhang, L. (deposition date: 2016-02-24, release date: 2016-12-14, Last modification date: 2024-10-23) |
| Primary citation | Nitsche, C.,Zhang, L.,Weigel, L.F.,Schilz, J.,Graf, D.,Bartenschlager, R.,Hilgenfeld, R.,Klein, C.D. Peptide-Boronic Acid Inhibitors of Flaviviral Proteases: Medicinal Chemistry and Structural Biology. J. Med. Chem., 60:511-516, 2017 Cited by PubMed Abstract: A thousand-fold affinity gain is achieved by introduction of a C-terminal boronic acid moiety into dipeptidic inhibitors of the Zika, West Nile, and dengue virus proteases. The resulting compounds have K values in the two-digit nanomolar range, are not cytotoxic, and inhibit virus replication. Structure-activity relationships and a high resolution X-ray cocrystal structure with West Nile virus protease provide a basis for the design of optimized covalent-reversible inhibitors aimed at emerging flaviviral pathogens. PubMed: 27966962DOI: 10.1021/acs.jmedchem.6b01021 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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