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. 2022 Apr 19;5:375. doi: 10.1038/s42003-022-03333-9

Fig. 3. R-domains of AT and PT do not bind HBEGF.

Fig. 3

a R-domain structural comparison highlighting conserved β-sandwich motif. The structure of DTR in complex with HBEGF (yellow) was generated from PDB entry 1XDT. The Ω-loop between β8 and β9, and the lid structure between β9 and β10 are labeled. b Dose titration of DT and DT R-domain chimeras DT(ATR), and DT(PTR) on Vero cells (mean ± SD, n = 3); n = 3 biological replicates. c Dose titration of DT, DT(ATR), and DT(PTR) on WT, HBEGFKO and +HBEGF cells (mean ± SD, n = 2); n = 3 biological replicates. DT sensitivity (EC50) tracked with expression of HBEGF (WT—26 pM, HBEGFKO-N/A, + HBEGF—0.43 pM). Sensitivity to DT(ATR) and DT(PTR) was unaffected by HBEGF expression (WT—169 and 25 nM, HBEGFKO—245 and 55 nM, +HBEGF—608 and 50 nM).