The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Crystal Structure of Argonaute and Its Implications for RISC Slicer Activity
Abstract
Argonaute proteins and small interfering RNAs (siRNAs) are the known signature components of the RNA interference effector complex RNA-induced silencing complex (RISC). However, the identity of “Slicer,” the enzyme that cleaves the messenger RNA (mRNA) as directed by the siRNA, has not been resolved. Here, we report the crystal structure of the Argonaute protein from Pyrococcus furiosus at 2.25 angstrom resolution. The structure reveals a crescent-shaped base made up of the amino-terminal, middle, and PIWI domains. The Piwi Argonaute Zwille (PAZ) domain is held above the base by a “stalk”-like region. The PIWI domain (named for the protein piwi) is similar to ribonuclease H, with a conserved active site aspartate-aspartate-glutamate motif, strongly implicating Argonaute as “Slicer.” The architecture of the molecule and the placement of the PAZ and PIWI domains define a groove for substrate binding and suggest a mechanism for siRNA-guided mRNA cleavage.
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Bartel (2004) · doi:10.1016/s0092-8674(04)00045-5 · Cited by 34,714
Potent and specific genetic interference by double-stranded RNA in Caenorhabditis elegans
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Recombining the structures of HIV integrase, RuvC and RNase H
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Kim, V. N., Han, J., & Siomi, M. C. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2632 · Cited by 2,814
Argonaute2 is the catalytic engine of mammalian RNAi
Liu, J., Carmell, M. A., Rivas, F. V., Marsden, C. G., Thomson, J. M., Song, J.-J., Hammond, S. M., Joshua-Tor, L., & Hannon, G. J. (2004) · Science · doi:10.1126/science.1102513 · Cited by 2,796
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Metadata
- Authors
- Song, J.-J., Smith, S. K., Hannon, G. J., & Joshua-Tor, L.
- Venue
- Science
- Published
- 2004-09-03
- Volume
- 305
- Issue
- 5689
- Pages
- 1434-1437
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2074106269
- Cited by
- 1,470
- References
- 4
- FWCI
- 35.53
- Type
- journal article
- Language
- en
- Open access
- closed
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