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. Author manuscript; available in PMC: 2024 Jan 1.
Published in final edited form as: Trends Biochem Sci. 2022 Jul 7:S0968-0004(22)00146-3. doi: 10.1016/j.tibs.2022.06.005

Figure 4. AGO adopts distinct conformations when engaged with canonical or TDMD-inducing targets.

Figure 4.

(A) When bound to a canonical target via base-pairing of the seed region, the miRNA 3′ end is buried in the PAZ domain of AGO (left panel; PDB: 4W5T) [10]. Interaction with a TDMD-inducing target with extended 3′ complementarity, however, exposes the miRNA 3′ end to solvent, which enables tailing and trimming (right panel; PDB: 6MDZ) [72]. Protein structures were rendered by UCSF ChimeraX [109]. (B) Canonical miRNA-target interactions involve base-pairing of the miRNA seed region with or without additional supplementary pairing [1]. A validated canonical binding site for miR-29b in the 3′ UTR of human COL1A1 is shown [110]. (C) Targets that induce TDMD base pair with the miRNA seed region, display extensive complementarity to the miRNA 3′ end, and have central mismatches. Interaction of miR-29b with a TDMD-inducing site in the 3′ UTR of human NREP is shown [82].