{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["15(1)"],"submitter":["Gao X"],"pubmed_abstract":["SETD3 is an essential host factor for the replication of a variety of enteroviruses that specifically interacts with viral protease 2A. However, the interaction between SETD3 and the 2A protease has not been fully characterized. Here, we use X-ray crystallography and cryo-electron microscopy to determine the structures of SETD3 complexed with the 2A protease of EV71 to 3.5 Å and 3.1 Å resolution, respectively. We find that the 2A protease occupies the V-shaped central cleft of SETD3 through two discrete sites. The relative positions of the two proteins vary in the crystal and cryo-EM structures, showing dynamic binding. A biolayer interferometry assay shows that the EV71 2A protease outcompetes actin for SETD3 binding. We identify key 2A residues involved in SETD3 binding and demonstrate t"],"journal":["Nature communications"],"pagination":["4176"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11099015"],"repository":["biostudies-literature"],"pubmed_title":["The EV71 2A protease occupies the central cleft of SETD3 and disrupts SETD3-actin interaction."],"pmcid":["PMC11099015"],"pubmed_authors":["Ding W","Wang B","Zhu K","Shang K","Gao X","Cui S","Wang J","Qin B","Wang L"],"additional_accession":[]},"is_claimable":false,"name":"The EV71 2A protease occupies the central cleft of SETD3 and disrupts SETD3-actin interaction.","description":"SETD3 is an essential host factor for the replication of a variety of enteroviruses that specifically interacts with viral protease 2A. However, the interaction between SETD3 and the 2A protease has not been fully characterized. Here, we use X-ray crystallography and cryo-electron microscopy to determine the structures of SETD3 complexed with the 2A protease of EV71 to 3.5 Å and 3.1 Å resolution, respectively. We find that the 2A protease occupies the V-shaped central cleft of SETD3 through two discrete sites. The relative positions of the two proteins vary in the crystal and cryo-EM structures, showing dynamic binding. A biolayer interferometry assay shows that the EV71 2A protease outcompetes actin for SETD3 binding. We identify key 2A residues involved in SETD3 binding and demonstrate t","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 May","modification":"2026-06-02T06:54:52.633Z","creation":"2026-04-15T03:15:19.851Z"},"accession":"S-EPMC11099015","cross_references":{"pubmed":["38755176"],"doi":["10.1038/s41467-024-48504-w"]}}