Summary information and primary citation
- PDB-id
-
1knz;
DSSR-derived features in text and
JSON formats; DNAproDB
- Class
- viral protein-RNA
- Method
- X-ray (2.45 Å)
- Summary
- Recognition of the rotavirus mrna 3' consensus by an
asymmetric nsp3 homodimer
- Reference
-
Deo RC, Groft CM, Rajashankar KR, Burley SK (2002):
"Recognition
of the rotavirus mRNA 3' consensus by an asymmetric NSP3
homodimer." Cell(Cambridge,Mass.),
108, 71-81. doi: 10.1016/S0092-8674(01)00632-8.
- Abstract
- Rotaviruses, the cause of life-threatening diarrhea in
humans and cattle, utilize a functional homolog of poly(A)
binding protein (PABP) known as nonstructural protein 3
(NSP3) for translation of viral mRNAs. NSP3 binds to viral
mRNA 3' consensus sequences and circularizes the mRNA via
interactions with eIF4G. The X-ray structure of the NSP3
RNA binding domain bound to a rotaviral mRNA 3' end has
been determined. NSP3 is a novel, heart-shaped homodimer
with a medial RNA binding cleft. The homodimer is
asymmetric, and contains two similar N-terminal segments
plus two structurally different C-terminal segments that
intertwine to create a tunnel enveloping the mRNA 3' end.
Biophysical studies demonstrate high affinity binding
leading to increased thermal stability and slow
dissociation kinetics, consistent with NSP3 function.
