1m1c

Structural highlights

Function

[GAG_SCVLA] Capsid protein self-assembles to form an icosahedral capsid with a T=2 symmetry, 40 nm in diameter, and consisting of 60 capsid proteins asymmetric dimers. The capsid encapsulates the genomic dsRNA and the polymerase and remains 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 the virion and are extruded into the cytoplasm.^{[1] [2]} Binds and removes 5' cap structures from cellular mRNA. Forms a covalent bond with m7GMP through His-154 of the capsid protein while releasing the mRNA body.^{[3] [4]}

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. ↑ Blanc A, Goyer C, Sonenberg N. The coat protein of the yeast double-stranded RNA virus L-A attaches covalently to the cap structure of eukaryotic mRNA. Mol Cell Biol. 1992 Aug;12(8):3390-8. PMID:1630453
2. ↑ Masison DC, Blanc A, Ribas JC, Carroll K, Sonenberg N, Wickner RB. Decoying the cap- mRNA degradation system by a double-stranded RNA virus and poly(A)- mRNA surveillance by a yeast antiviral system. Mol Cell Biol. 1995 May;15(5):2763-71. PMID:7739557
3. ↑ Blanc A, Goyer C, Sonenberg N. The coat protein of the yeast double-stranded RNA virus L-A attaches covalently to the cap structure of eukaryotic mRNA. Mol Cell Biol. 1992 Aug;12(8):3390-8. PMID:1630453
4. ↑ Masison DC, Blanc A, Ribas JC, Carroll K, Sonenberg N, Wickner RB. Decoying the cap- mRNA degradation system by a double-stranded RNA virus and poly(A)- mRNA surveillance by a yeast antiviral system. Mol Cell Biol. 1995 May;15(5):2763-71. PMID:7739557
5. ↑ Naitow H, Tang J, Canady M, Wickner RB, Johnson JE. L-A virus at 3.4 A resolution reveals particle architecture and mRNA decapping mechanism. Nat Struct Biol. 2002 Oct;9(10):725-8. PMID:12244300 doi:10.1038/nsb844