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	Differential inhibition of Morbillivirus and Henipavirus polymerases by ERDRP-0519 and structure-guided inhibitor optimization.
Journal, issue, pages	Cell, Year 2026
Publish date	Apr 29, 2026
Authors	Lu Xue / Jiacheng Gui / Shenghua Gao / Xiaoxiao Gao / Tiancai Chang / Hainei Pan / Jielin Tang / Mingxia Zhang / Zimu Li / Binqian Zou / Heyu Zhao / Longyu Wang / Mei Li / Lijun Rong / Richard K Plemper / Xinwen Chen / Jun He / Rongjuan Pei / Peng Zhan / Xiaoli Xiong /
PubMed Abstract	ERDRP-0519 is a non-nucleoside polymerase inhibitor developed against measles virus (MeV) of the Morbillivirus genus. Here, we show that ERDRP-0519 also cross-inhibits Nipah virus (NiV) of the ...ERDRP-0519 is a non-nucleoside polymerase inhibitor developed against measles virus (MeV) of the Morbillivirus genus. Here, we show that ERDRP-0519 also cross-inhibits Nipah virus (NiV) of the Henipavirus genus with reduced potency. ERDRP-0519 binds to a shared pocket within the RNA-dependent RNA polymerase (RdRp) palm domains of MeV, peste des petits ruminants virus (PPRV), and NiV polymerases. ERDRP-0519 forms more extensive interactions with Morbillivirus polymerases, whereas binding to NiV polymerase requires substantial RdRp motif rearrangements, likely incurring an energetic cost and resulting in reduced affinity. ERDRP-0519 binding impedes RNA synthesis by sterically blocking RNA and nucleotide binding. Guided by these insights, we designed GL22 and G671, ERDRP-0519 derivatives with extended moieties that engage additional cross-domain RdRp contacts in the NiV polymerase. These derivatives exert more extensive steric hindrance to RNA and nucleotide binding, enhancing biochemical inhibition potency. These findings elucidate the molecular mechanism of ERDRP-0519 action and guide structure-based inhibitor design.
External links	Cell / PubMed:42061399
Methods	EM (single particle)
Resolution	2.4 - 2.92 Å
Structure data	65442 9vxv EMDB-65442, PDB-9vxv: Cryo-EM Structure of Nipah Virus Polymerase in complex with ERDRP-0519 Method: EM (single particle) / Resolution: 2.66 Å 65444 9vxx EMDB-65444, PDB-9vxx: Cryo-EM Structure of Measles Virus Polymerase in complex with ERDRP-0519 Method: EM (single particle) / Resolution: 2.73 Å 65445 9vxy EMDB-65445, PDB-9vxy: Cryo-EM Structure of Nipah Virus Polymerase in complex with GL22 Method: EM (single particle) / Resolution: 2.87 Å 65446 9vxz EMDB-65446, PDB-9vxz: Cryo-EM structure of Measles Virus L Protein bound by Phosphoprotein Tetramer Method: EM (single particle) / Resolution: 2.68 Å 65447 9vy0 EMDB-65447, PDB-9vy0: Cryo-EM Structure of Peste Des Petits Ruminants Virus Polymerase in complex with ERDRP-0519 Method: EM (single particle) / Resolution: 2.71 Å 65448 9vy1 EMDB-65448, PDB-9vy1: Cryo-EM structure of Peste Des Petits Ruminants Virus L Protein bound by Phosphoprotein Tetramer Method: EM (single particle) / Resolution: 2.4 Å 68072 21xo EMDB-68072, PDB-21xo: Cryo-EM Structure of Nipah Virus Polymerase in complex with G671 Method: EM (single particle) / Resolution: 2.92 Å
Chemicals	PDB-1e3h: SeMet derivative of Streptomyces antibioticus PNPase/GPSI enzyme ChemComp-ZN: Unknown entry PDB-1ef9: THE CRYSTAL STRUCTURE OF METHYLMALONYL COA DECARBOXYLASE COMPLEXED WITH 2S-CARBOXYPROPYL COA PDB-1et4: CRYSTAL STRUCTURE OF A VITAMIN B12 BINDING RNA APTAMER WITH LIGAND AT 2.3 A
Source	henipavirus nipahense measles morbillivirus measles virus genotype b3 peste-des-petits-ruminants virus
Keywords	VIRAL PROTEIN / Polymerase / inhibitor / nipah virus / complex / REPLICATION / Measles virus / RNA / Peste Des Petits Ruminants Virus