Fig. 3 | Nature Communications

Fig. 3

From: Structural basis for terminal loop recognition and stimulation of pri-miRNA-18a processing by hnRNP A1

Fig. 3The alternative text for this image may have been generated using AI.

Structure of the UP1/12-mer complex. a Schematic representation of the 2:2 UP1/12-mer RNA complex observed in the crystal structure (Supplementary Fig. 4a) and the proposed 1:1 complex in solution. b Static light scattering (SLS) profiles of UP1, pri-mir-18a, UP1/12-mer, and UP1/pri-mir-18a. The molecular weight (MW) obtained from SLS is indicated. UP1 forms a 1:1 complex with both pri-mir-18a and the 12-mer oligonucleotide. c Structural model of the 1:1 UP1/12-mer complex, where each RRM domain recognizes a UAG motif in the 12-mer RNA (magenta) forming a 1:1 complex. d Structural details of recognition of the UAG motif by RRM1 and RRM2 domains. Side-chain of selected residues involved in the interaction are indicated. e, f Correlation of experimental 1H-15N residual dipolar couplings (RDCs) (e) and small angle X-ray scattering (SAXS) data (f) vs. those calculated from the structural model shown in c

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