3QX8
Crystal structure of MID domain from hAGO2 in complex with m7GpppG
Summary for 3QX8
Entry DOI | 10.2210/pdb3qx8/pdb |
Related | 3LUC |
Descriptor | Protein argonaute-2, 7-METHYL-GUANOSINE-5'-TRIPHOSPHATE-5'-GUANOSINE (3 entities in total) |
Functional Keywords | rossmann-like folde, rna binding, small rna, rna binding protein |
Biological source | Homo sapiens (human) |
Cellular location | Cytoplasm, P-body: Q9UKV8 |
Total number of polymer chains | 3 |
Total formula weight | 48388.18 |
Authors | Frank, F.,Fabian, M.R.,Stepinski, J.,Jemielity, J.,Darzynkiewicz, E.,Sonenberg, N.,Nagar, B. (deposition date: 2011-03-01, release date: 2011-04-20, Last modification date: 2023-09-13) |
Primary citation | Frank, F.,Fabian, M.R.,Stepinski, J.,Jemielity, J.,Darzynkiewicz, E.,Sonenberg, N.,Nagar, B. Structural analysis of 5'-mRNA-cap interactions with the human AGO2 MID domain. Embo Rep., 12:415-420, 2011 Cited by PubMed Abstract: In RNA silencing, microRNA (miRNA)-mediated translational repression occurs through mechanisms that do not invoke messenger-RNA (mRNA) target cleavage by Argonaute proteins. The nature of these mechanisms is unclear, but several recent studies have proposed that a direct interaction between the mRNA-cap and the middle (MID) domain of Argonautes is involved. Here, we present crystallographic and NMR data demonstrating that cap analogues do not bind significantly to the isolated MID domain of human Argonaute 2 (hAGO2) and are found in the miRNA 5'-nucleotide binding site in an implausible binding mode. Additionally, in vitro pull-down experiments with full-length hAGO2 indicate that the interaction with cap analogues is nonspecific. PubMed: 21475248DOI: 10.1038/embor.2011.48 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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