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9KNV

AS-136A-bound measles virus L-P complex

This is a non-PDB format compatible entry.
Summary for 9KNV
Entry DOI10.2210/pdb9knv/pdb
EMDB information62459 62463
DescriptorRNA-directed RNA polymerase L, Phosphoprotein, ZINC ION, ... (4 entities in total)
Functional Keywordscomplex, transcription, as-136a, measles virus, l-p complex, polymerase complex
Biological sourceMeasles virus strain Ichinose-B95a
More
Total number of polymer chains4
Total formula weight410487.53
Authors
Wang, Y.R.,Zhang, H.Q. (deposition date: 2024-11-19, release date: 2025-07-16, Last modification date: 2025-07-23)
Primary citationWang, Y.,Zhao, L.,Zhang, Y.,Gao, X.,Wang, Y.,Shi, W.,Kornberg, R.D.,Zhang, H.
Structures of the measles virus polymerase complex with non-nucleoside inhibitors and mechanism of inhibition.
Cell, 2025
Cited by
PubMed Abstract: The measles virus (MeV), a highly contagious non-segmented negative-sense RNA virus in the Paramyxoviridae family, causes millions of infections annually, with no approved antivirals available. The viral polymerase complex, comprising the large (L) protein and the tetrameric phosphoprotein (P), is a key antiviral target. We determined the cryo-electron microscopy structures of the MeV polymerase complex alone and bound to two non-nucleoside inhibitors, ERDRP-0519 and AS-136A. Inhibitor binding induces a conformational change in the catalytic loop, allosterically locking the polymerase in an inactive "GDN-out" state. These findings led to the proposal that ERDRP-0519 would also be effective against Nipah virus (NiV), a highly pathogenic virus with no available antivirals. This proposal was confirmed by structure determination of the NiV polymerase complex and by inhibition of transcription.
PubMed: 40628260
DOI: 10.1016/j.cell.2025.06.017
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.3 Å)
Structure validation

239149

數據於2025-07-23公開中

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