Please use this identifier to cite or link to this item: https://doi.org/10.1038/embor.2008.118
Title: Structural basis for RNA-silencing suppression by Tomato aspermy virus protein 2b
Authors: Chen, H.-Y.
Yang, J.
Lin, C. 
Yuan, Y.A. 
Issue Date: 2008
Citation: Chen, H.-Y., Yang, J., Lin, C., Yuan, Y.A. (2008). Structural basis for RNA-silencing suppression by Tomato aspermy virus protein 2b. EMBO Reports 9 (8) : 754-760. ScholarBank@NUS Repository. https://doi.org/10.1038/embor.2008.118
Abstract: The 2b proteins encoded by cucumovirus act as post-transcriptional gene silencing suppressors to counter host defence during infection. Here we report the crystal structure of Tomato aspermy virus 2b (TAV2b) protein bound to a 19 bp small interfering RNA (siRNA) duplex. TAV2b adopts an all α-helix structure and forms a homodimer to measure siRNA duplex in a length-preference mode. TAV2b has a pair of hook-like structures to recognize simultaneously two α-helical turns of A-form RNA duplex by fitting its α-helix backbone into two adjacent major grooves of siRNA duplex. The conserved π-stackings between tryptophan and the 5′-terminal base of siRNA duplex from both ends enhance the recognition. TAV2b further oligomerizes to form a dimer of dimers through the conserved leucine-zipper-like motif at its amino-terminal α-helix. Biochemical experiments suggest that TAV2b might interfere with the post-transcriptional gene silencing pathway by directly binding to siRNA duplex.
Source Title: EMBO Reports
URI: http://scholarbank.nus.edu.sg/handle/10635/101747
ISSN: 1469221X
DOI: 10.1038/embor.2008.118
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