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8ZPV

Nipah virus polymerase complex

Summary for 8ZPV
Entry DOI10.2210/pdb8zpv/pdb
EMDB information60355
DescriptorRNA-directed RNA polymerase L, Phosphoprotein, ZINC ION (3 entities in total)
Functional Keywordspolymerase, virus, transcription, nipah
Biological sourceHenipavirus nipahense
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Total number of polymer chains5
Total formula weight571229.22
Authors
Wang, Y.R.,Zhang, H.Q. (deposition date: 2024-05-31, release date: 2024-11-13, Last modification date: 2024-12-25)
Primary citationWang, Y.,Zhao, L.,Zhang, Y.,Wang, Y.,Tang, J.,Liu, S.,Gao, H.,Zhang, X.,Zinzula, L.,Kornberg, R.D.,Zhang, H.
Cryo-EM structure of Nipah virus RNA polymerase complex.
Sci Adv, 10:eadr7116-eadr7116, 2024
Cited by
PubMed Abstract: Nipah virus, a member of the family, is a highly pathogenic nonsegmented, negative-sense RNA virus (nsNSV) which causes severe neurological and respiratory illnesses in humans. There are no available drugs or vaccines to combat this virus. A complex of large polymerase protein (L) and phosphoprotein (P) of Nipah virus supports replication and transcription and affords a target for antiviral drug development. Structural information required for drug development is lacking. Here we report the 2.9-angstrom cryo-electron microscopy structure of the Nipah virus polymerase-phosphoprotein complex. The structure identifies conserved amino acids likely important for recognition of template RNA by nsNSVs and reveals the locations of mutation-prone sites among Nipah virus strains, which may facilitate the development of therapeutic agents against Nipah virus by targeting regions unaffected by these mutation sites.
PubMed: 39661676
DOI: 10.1126/sciadv.adr7116
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.9 Å)
Structure validation

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