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Recognition of the Rotavirus mRNA 3′ Consensus by an Asymmetric NSP3 Homodimer

By Rahul C. Deo, Caroline M. Groft, K.R. Rajashankar and Stephen K. Burley

Abstract

AbstractRotaviruses, 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

Publisher: Cell Press.
Year: 2002
DOI identifier: 10.1016/S0092-8674(01)00632-8
OAI identifier:

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