期刊
CELL
卷 150, 期 1, 页码 100-110出版社
CELL PRESS
DOI: 10.1016/j.cell.2012.05.017
关键词
-
资金
- Department of Energy, Office of Basic Energy Sciences
- Jane Coffin Childs Memorial Fund for Medical Research Fellowship
- Louis Morin Charitable Trust
- [GM062534]
Argonaute proteins lie at the heart of the RNA-induced silencing complex (RISC), wherein they use small RNA guides to recognize targets. Initial insight into the architecture of Argonautes came from studies of prokaryotic proteins, revealing a crescent-shaped base made up of the amino-terminal, PAZ, middle, and PIWI domains. The recently reported crystal structure of human Argonaute-2 (hAgo2), the slicer in RNA interference, in complex with a mixed population of RNAs derived from insect cells provides insight into the architecture of a eukaryotic Argonaute protein with defined biochemical and biological functions. Here, we report the structure of human Ago2 bound to a physiologically relevant microRNA, microRNA-20a, at 2.2 angstrom resolution. The miRNA is anchored at both ends by the Mid and PAZ domains and makes several kinks and turns along the binding groove. Interestingly, miRNA binding confers remarkable stability on hAgo2, locking this otherwise flexible enzyme into a stable conformation.
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