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. Author manuscript; available in PMC: 2024 Nov 1.
Published in final edited form as: Nat Chem Biol. 2023 Aug 31;19(11):1423–1431. doi: 10.1038/s41589-023-01422-2

Figure 1. ProP-PD screening identified a specific OGT binding motif.

Figure 1.

(a) Domain schematic of full-length OGT with tetratricopeptide repeat (TPR) domain in gray, N-terminal catalytic (N-Cat) domain in green, intervening domain (Int-D) in blue, and C-terminal catalytic (C-Cat) domain in yellow. The crystallization construct OGT4.5 with only 4.5 of 13.5 TPR repeats was also shown. (b) Sequence logo of highly enriched peptides from both OGT and OGT4.5 ProP-PD screens, aligned to the PxYx[I/L] motif. (c) Microscale thermophoresis (MST) binding assay of SMG9 peptide with OGT, n=3. (d) Competitive fluorescence polarization (FP) binding assay with fluorescently labeled 5-FAM-SMG9 peptide competing with unmodified SMG9, ZNF831, and consensus peptide 37 (CP37), for OGT binding, n=3. Data are presented as mean values +/− SD of three replicates.