2X04
Crystal structure of the PABC-TNRC6C complex
Summary for 2X04
Entry DOI | 10.2210/pdb2x04/pdb |
Related | 1CVJ 1G9L 1JGN 1JH4 2DKL |
Descriptor | POLYADENYLATE-BINDING PROTEIN 1, TRINUCLEOTIDE REPEAT-CONTAINING GENE 6C PROTEIN, SULFATE ION, ... (4 entities in total) |
Functional Keywords | peptide-rna binding protein complex, rna-mediated gene silencing, nucleus, methylation, spliceosome, translation regulation, protein-protein complex, coiled coil, deadenylation, mrna splicing, phosphoprotein, mrna processing, microrna silencing, peptide/rna binding protein |
Biological source | HOMO SAPIENS (HUMAN) More |
Cellular location | Cytoplasm: P11940 |
Total number of polymer chains | 4 |
Total formula weight | 21566.78 |
Authors | Jinek, M.,Fabian, M.R.,Coyle, S.M.,Sonenberg, N.,Doudna, J.A. (deposition date: 2009-12-04, release date: 2010-01-19, Last modification date: 2024-05-08) |
Primary citation | Jinek, M.,Fabian, M.R.,Coyle, S.M.,Sonenberg, N.,Doudna, J.A. Structural Insights Into the Human Gw182-Pabc Interaction in Microrna-Mediated Deadenylation Nat.Struct.Mol.Biol., 17:238-, 2010 Cited by PubMed Abstract: GW182-family proteins are essential for microRNA-mediated translational repression and deadenylation in animal cells. Here we show that a conserved motif in the human GW182 paralog TNRC6C interacts with the C-terminal domain of polyadenylate binding protein 1 (PABC) and present the crystal structure of the complex. Mutations at the complex interface impair mRNA deadenylation in mammalian cell extracts, suggesting that the GW182-PABC interaction contributes to microRNA-mediated gene silencing. PubMed: 20098421DOI: 10.1038/NSMB.1768 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.49 Å) |
Structure validation
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