Summary for 4OLB
| Entry DOI | 10.2210/pdb4olb/pdb |
| Related | 4OLA |
| Descriptor | Protein argonaute-2, 5'-R(P*AP*AP*AP*AP*AP*AP*AP*AP*AP*U)-3', TRYPTOPHAN, ... (4 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 | 101010.69 |
| Authors | Schirle, N.T.,MacRae, I.J. (deposition date: 2014-01-23, release date: 2014-02-05, Last modification date: 2023-09-20) |
| Primary citation | Schirle, N.T.,MacRae, I.J. The crystal structure of human Argonaute2. Science, 336:1037-1040, 2012 Cited by 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: 22539551DOI: 10.1126/science.1221551 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.899 Å) |
Structure validation
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