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. Author manuscript; available in PMC: 2021 Mar 25.
Published in final edited form as: Nat Chem Biol. 2018 Jan 15;14(3):284–290. doi: 10.1038/nchembio.2551

Figure 6 ∣. Representation of key interactions responsible for high affinity binding of DAKD to B1R and of BK to B2R.

Figure 6 ∣

B1R discriminates between DAKD and BK mainly via electrostatic interactions at the N terminus, whereas B2R selects via a complex interaction network as a result of different C-terminal structures of the BK and DAKD. The residues conserved among B1R and B2R are shown in bold circles.