The enterovirus genus of the Picornaviridae family includes numerous pathogenic viruses responsible for many human diseases, such as the common cold, poliomyelitis, acute flaccid paralysis, and myocarditis. These viruses contain a (+)-sense single-stranded RNA genome with about 7500 nucleotides (nts), which is polyadenylated at the 3′-end and linked covalently with viral protein VPg at the 5′-end. The entire genome consists of a single open reading frame (ORF) flanked by the highly conserved 5′ and 3′ untranslated regions (UTRs). The ~750-nt 5′-UTR harbors modular RNA domains essential for the viral genome translation and replication within the host cells. The extreme 5′-end of the enterovirus RNA genome contains a conserved cloverleaf-like domain that recruits 3CD and PCBP proteins required for initiating genome replication. Here, we report the crystal structure at 1.9 Å resolution of this domain from the CVB3 genome in complex with an antibody chaperone. The RNA folds into an antiparallel H-type four-way junction comprising four subdomains with co-axially stacked sA-sD and sB-sC helices, as you can see from this X-ray structure (PDB code: 8DP3)

#molecularart ... #immolecular ... #virus ... #genome ... #RNA ... #cloverleaf ... #replication ... #xray ... #enterovirus

Structure rendered with @proteinimaging and depicted with @corelphotopaint