Summary information and primary citation
- PDB-id
-
1rpu;
DSSR-derived features in text and
JSON formats; DNAproDB
- Class
- RNA binding protein-RNA
- Method
- X-ray (2.5 Å)
- Summary
- Crystal structure of cirv p19 bound to sirna
- Reference
-
Vargason JM, Szittya G, Burgyan J, Hall TMT (2003):
"Size
selective recognition of siRNA by an RNA silencing
suppressor." Cell(Cambridge,Mass.),
115, 799-811. doi: 10.1016/S0092-8674(03)00984-X.
- Abstract
- RNA silencing in plants likely exists as a defense
mechanism against molecular parasites such as RNA viruses,
retrotransposons, and transgenes. As a result, many plant
viruses have adapted mechanisms to evade and suppress gene
silencing. Tombusviruses express a 19 kDa protein (p19),
which has been shown to suppress RNA silencing in vivo and
bind silencing-generated and synthetic small interfering
RNAs (siRNAs) in vitro. Here we report the 2.5 A crystal
structure of p19 from the Carnation Italian ringspot virus
(CIRV) bound to a 21 nt siRNA and demonstrate in
biochemical and in vivo assays that CIRV p19 protein acts
as a molecular caliper to specifically select siRNAs based
on the length of the duplex region of the RNA.
