Summary for 9JQK
| Entry DOI | 10.2210/pdb9jqk/pdb |
| Descriptor | Transcriptional activator VP30, 2-[(~{E})-heptadec-10-enyl]-6-oxidanyl-benzoic acid, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | vp30, viral protein |
| Biological source | Ebola virus (ZEBOV, Zaire Ebola virus) |
| Total number of polymer chains | 4 |
| Total formula weight | 74042.44 |
| Authors | |
| Primary citation | Peng, C.,Wu, F.,Ma, Y.,Liu, G.,Huang, Y.,Tong, R.,Xu, W. Ginkgolic acid inhibits Ebola virus transcription and replication by disrupting the interaction between nucleoprotein and VP30 protein. Antiviral Res., 234:106074-106074, 2025 Cited by PubMed Abstract: The Ebola virus, a filovirus, has been responsible for significant human fatalities since its discovery. Despite extensive research, effective small-molecule drugs remain elusive due to its complex pathogenesis. Inhibition of RNA synthesis is a promising therapeutic target, and the VP30 protein plays a critical role in this process. The interaction between VP30 and the nucleoprotein (NP) is essential for viral replication. We identified ginkgolic acid as a small molecule with strong affinity for VP30, which was validated through multiple assays, including thermal shift, surface plasmon resonance, fluorescence polarization, pull-down, and co-immunoprecipitation. The antiviral efficacy of ginkgolic acid was demonstrated in the EBOV transcription- and replication-competent virus-like particle (trVLP) system. Furthermore, we resolved the crystal structure of the VP30-ginkgolic acid complex, revealing two ginkgolic acid molecules located at the VP30/NP interaction interface. This structural information provides insight into the molecular basis of ginkgolic acid's antiviral activity and suggests a novel therapeutic strategy targeting the VP30/NP interaction. PubMed: 39716669DOI: 10.1016/j.antiviral.2024.106074 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.29 Å) |
Structure validation
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