3gzu

Structural highlights

Function

[VP2_ROTW3] Inner capsid protein that self assembles to form an icosahedral capsid with a T=2 symmetry, which consists of 120 copies of VP2, with channels at each of its five-fold vertices. This capsid constitutes the innermost concentric layer of the viral mature particle. It encapsidates the polymerase VP1, the capping enzyme VP3 and the genomic dsRNA, thereby defining the core. The innermost VP2 capsid and the intermediate VP6 capsid remain intact following cell entry to protect the dsRNA from degradation and to prevent unfavorable antiviral responses in the host cell during all the replication cycle of the virus. Nacent transcripts are transcribed within the structural confines of this double-layered particle (DLP) and are extruded through the channels at the five-fold axes. VP2 is required for the replicase activity of VP1 polymerase. It probably plays a role in the coordination of packaging and genome replication by controlling the initiation of minus-strand synthesis. Binding to the polymerase VP1 presumably activates the autoinhibited VP1-RNA complex which will start the synthesis of the complementary minus-strand (By similarity). [VP6_ROTRF] Intermediate capsid protein that self assembles to form an icosahedral capsid with a T=13 symmetry, which consists of 230 trimers of VP6, with channels at each of its five-fold vertices. This capsid constitutes the middle concentric layer of the viral mature particle. The innermost VP2 capsid and the intermediate VP6 capsid remain intact following cell entry to protect the dsRNA from degradation and to prevent unfavorable antiviral responses in the host cell during all the replication cycle of the virus. Nacent transcripts are transcribed within the structural confines of this double-layered particle (DLP) and are extruded through the channels at the five-fold axes. VP6 is required for the transcription activity of the DLP.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

• Virus coat protein

References

1. ↑ Bican P, Cohen J, Charpilienne A, Scherrer R. Purification and characterization of bovine rotavirus cores. J Virol. 1982 Sep;43(3):1113-7. PMID:6292454
2. ↑ Chen JZ, Settembre EC, Aoki ST, Zhang X, Bellamy AR, Dormitzer PR, Harrison SC, Grigorieff N. Molecular interactions in rotavirus assembly and uncoating seen by high-resolution cryo-EM. Proc Natl Acad Sci U S A. 2009 Jun 30;106(26):10644-8. Epub 2009 Jun 1. PMID:19487668