4OLA

Crystal Structure of Human Argonaute2

Replaces:  4EI1

Summary for 4OLA

• Entry DOI: 10.2210/pdb4ola/pdb
• Related: 4OLB
• Descriptor: Protein argonaute-2, 5'-R(P*AP*AP*AP*AP*AP*AP*AP*AP*AP*U)-3', PHENOL, ... (5 entities in total)
• Functional Keywords: rna-binding protein, rna interference, protein-rna complex, ago, hydrolase-rna complex, hydrolase/rna
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm, P-body: Q9UKV8
• Total number of polymer chains: 2
• Total formula weight: 100756.45

Authors

Schirle, N.T.,MacRae, I.J. (deposition date: 2014-01-23, release date: 2014-02-05, Last modification date: 2024-02-28)

Primary citation

Schirle, N.T.,MacRae, I.J.
The crystal structure of human Argonaute2.
Science, 336:1037-1040, 2012

PubMed Abstract: 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.

PubMed: 22539551
DOI: 10.1126/science.1221551

Experimental method

X-RAY DIFFRACTION (2.3 Å)