Fig. 5: Mutations to complementary charged residues at the I358/I360 site in WRKY33_C and V51 in SIB1 restore interaction. | Communications Biology

Fig. 5: Mutations to complementary charged residues at the I358/I360 site in WRKY33_C and V51 in SIB1 restore interaction.

From: Structural basis for the regulation of plant transcription factor WRKY33 by the VQ protein SIB1

Fig. 5

a, b Overlay of the 1H-15N HSQC spectra of 15N-labeled WRKY33_C-I358D (a) or WRKY33_C-I360D (b) mutants in their free states (blue) and in the presence of the SIB1mini-V51R mutant peptide (red). The spectrum of 15N-labeled wild-type WRKY33_C in complex with wild-type SIB1mini peptide is shown for comparison (black). Enlarged view of the spectral changes for representative resonances are shown on the right.

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