期刊
SCIENCE
卷 336, 期 6084, 页码 1037-1040出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1221551
关键词
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资金
- National Institute of General Medical Sciences (NIGMS) Protein Structure Initiative [U54 GM074898]
- NIGMS [R01 GM086701]
Argonaute proteins form the functional core of the RNA-induced silencing complexes that mediate RNA silencing in eukaryotes. The 2.3 angstrom resolution crystal structure of human Argonaute2 (Ago2) reveals a bilobed molecule with a central cleft for binding guide and target RNAs. Nucleotides 2 to 6 of a heterogeneous mixture of guide RNAs are positioned in an A-form conformation for base pairing with target messenger RNAs. Between nucleotides 6 and 7, there is a kink that may function in microRNA target recognition or release of sliced RNA products. Tandem tryptophan-binding pockets in the PIWI domain define a likely interaction surface for recruitment of glycine-tryptophan-182 (GW182) or other tryptophan-rich cofactors. These results will enable structure-based approaches for harnessing the untapped therapeutic potential of RNA silencing in humans.
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