Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structural insights into measles virus RNA synthesis regulation and pan-paramyxoviral polymerase inhibition by ERDRP-0519.
Journal, issue, pages	Proc Natl Acad Sci U S A, Vol. 123, Issue 15, Page e2522978123, Year 2026
Publish date	Apr 14, 2026
Authors	Tianjiao Du / Jiening Wang / Chengji Yang / Rubing Xue / Ying Chen / Kaiyue Jie / Xiaokang Zhang / Long Zhang / Gaojie Song / Qiansen Zhang / Shan Wu / Heng Ru /
PubMed Abstract	Nonsegmented negative-sense RNA viruses (nsNSVs) rely on a multifunctional RNA-dependent RNA polymerase (RdRP) complex for transcription and replication. In measles virus (MeV), the nonstructural ...Nonsegmented negative-sense RNA viruses (nsNSVs) rely on a multifunctional RNA-dependent RNA polymerase (RdRP) complex for transcription and replication. In measles virus (MeV), the nonstructural protein C has long been implicated in regulating RNA synthesis, yet its precise role remains unclear. Here, we show that the MeV C protein directly associates with the RdRP complex. Using cryoelectron microscopy, we determined atomic-resolution structures of the MeV polymerase with and without C, revealing that C binding stabilizes the C-terminal region of L and locks the complex into a replication-competent elongation state. Biochemical data further show that C promotes N protein recruitment, enhancing polymerase processivity through facilitating encapsidation during replication. Additionally, we also resolved high-resolution structures of MeV and Nipah virus (NiV) polymerases bound to ERDRP-0519, an orally available morbillivirus inhibitor. Unexpectedly, the compound occupies an allosteric pocket within the RdRp domain rather than the previously predicted PRNTase domain, overlapping conserved resistance sites. This binding induces conformational changes in palm subdomain, blocking RNA template and nucleotide engagement, thereby halting RNA synthesis. These findings uncover distinct regulatory and inhibitory mechanisms in paramyxovirus polymerases and provide a structural framework for the rational design of broad-spectrum antivirals targeting MeV, NiV, and potentially other clinically relevant nsNSVs.
External links	Proc Natl Acad Sci U S A / PubMed:41941628 / PubMed Central
Methods	EM (single particle)
Resolution	2.6 - 3.17 Å
Structure data	65364 9vui EMDB-65364, PDB-9vui: Cryo-EM structure of the human measles virus RNA-dependent RNA polymerase complex bound to viral protein C Method: EM (single particle) / Resolution: 2.72 Å 65365 9vuj EMDB-65365, PDB-9vuj: Cryo-EM structure of the human measles virus RNA-dependent RNA polymerase Method: EM (single particle) / Resolution: 2.6 Å 65366 9vuk EMDB-65366, PDB-9vuk: Cryo-EM structure of the human measles virus RNA-dependent RNA polymerase complex Method: EM (single particle) / Resolution: 3.17 Å 65367 9vul EMDB-65367, PDB-9vul: Cryo-EM structure of the human measles virus RNA-dependent RNA polymerase bound to allosteric inhibitor ERDRP-0519 Method: EM (single particle) / Resolution: 3.13 Å 65368 9vum EMDB-65368, PDB-9vum: Cryo-EM structure of the Nipah virus RNA-dependent RNA polymerase complex bound to allosteric inhibitor ERDRP-0519 Method: EM (single particle) / Resolution: 2.84 Å
Chemicals	ChemComp-ZN: Unknown entry ChemComp-HOH: WATER PDB-1ef9: THE CRYSTAL STRUCTURE OF METHYLMALONYL COA DECARBOXYLASE COMPLEXED WITH 2S-CARBOXYPROPYL COA
Source	measles virus genotype a-vaccine synthetic construct (others) aequorea victoria (jellyfish) Nipah virus henipavirus nipahense escherichia coli k-12 (bacteria)
Keywords	VIRAL PROTEIN / Measles virus RNA-dependent RNA polymerase complex bound to viral protein C / Measles virus RNA-dependent RNA polymerase complex / Measles virus RNA-dependent RNA polymerase complex bound to allosteric inhibitor ERDRP-0519 / RNA-dependent RNA polymerase complex bound to allosteric inhibitor ERDRP-0519