3QX9

Crystal structure of MID domain from hAGO2 in complex with ATP

Summary for 3QX9

• Entry DOI: 10.2210/pdb3qx9/pdb
• Related: 3LUC 3QX8
• Descriptor: Protein argonaute-2, ADENOSINE-5'-TRIPHOSPHATE (3 entities in total)
• Functional Keywords: rossmann-like fold, rna binding protein
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm, P-body: Q9UKV8
• Total number of polymer chains: 3
• Total formula weight: 47499.41

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: 2024-02-21)

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

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: 21475248
DOI: 10.1038/embor.2011.48

Experimental method

X-RAY DIFFRACTION (2 Å)