Extended Data Fig. 10: Structure of MG aptamer bound with TMR. | Nature Chemical Biology

Extended Data Fig. 10: Structure of MG aptamer bound with TMR.

From: Structural basis of a small monomeric Clivia fluorogenic RNA with a large Stokes shift

Extended Data Fig. 10

(a-b) The tertiary structure of MG aptamer bound with TMR (PDB:1F1T) is shown in cartoon (a) and schematic (b). The RNA folds in helical architecture with TMR intercalates in the center. (c-d) Two A-minor base triples forming in the junction of MG aptamer are shown in stick. (e) Chemical structure of TMR. (f-h) Residues interaction lining TMR binding pocket of MG aptamer are shown in stick. One base tetrad (g) and one base pair G8-C28 (f) stack on both sides of the bound TMR. (i) In vitro fluorescence assay of NBSI binding with Clivia and MG aptamer, respectively. MG aptamer cannot activate the fluorescence of NBSI. Three experiments were carried out independently. Data represent the mean ± s.d. from three replicates.

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