8a5t
From Proteopedia
(Difference between revisions)
Line 9: | Line 9: | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/GAG_SCVLA 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.<ref>PMID:1630453</ref> <ref>PMID:7739557</ref> 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.<ref>PMID:1630453</ref> <ref>PMID:7739557</ref> | [https://www.uniprot.org/uniprot/GAG_SCVLA 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.<ref>PMID:1630453</ref> <ref>PMID:7739557</ref> 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.<ref>PMID:1630453</ref> <ref>PMID:7739557</ref> | ||
+ | |||
+ | ==See Also== | ||
+ | *[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> |
Current revision
Capsid structure of the L-A helper virus from native viral communities
|