Structural highlights
Function
POLG_HPE1H Capsid proteins VP0, VP2, VP3 form a closed capsid enclosing the viral positive strand RNA genome. Capsid proteins interact with host alpha-V/beta-3 integrin heterodimer to provide virion attachment target cell. This attachment induces virion internalization predominantly through clathrin-mediated endocytosis.[1] Protein 2A: Is not a protease. Protein 2B: Affects membrane integrity and cause an increase in membrane permeability. Protein 2C: Associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities (By similarity). Protein 3A, via its hydrophobic domain, serves as membrane anchor. Protease 3C: cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind cooperatively to the protease (By similarity). RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals.[PROSITE-ProRule:PRU00539]
References
- ↑ Joki-Korpela P, Marjomaki V, Krogerus C, Heino J, Hyypia T. Entry of human parechovirus 1. J Virol. 2001 Feb;75(4):1958-67. PMID:11160695 doi:http://dx.doi.org/10.1128/JVI.75.4.1958-1967.2001
