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. Author manuscript; available in PMC: 2023 Feb 8.
Published in final edited form as: Structure. 2021 Mar 11;29(7):768–777.e2. doi: 10.1016/j.str.2021.02.005

Figure 5. Structural ensembles of the RBD-CRD interactions with KD for B-Raf autoinhibition in the absence of the14-3-3 dimer.

Figure 5.

(A) The superimposed structures indicate that the RBD-CRD exhibits a potential to interact with the KD.

(B and C) The residue-based contacting probabilities of (B) RBD-CRD and (C) KD suggest a preference of CRD and KD’s N lobe for the RBD-CRD interactions with KD. The implicated activating residues in CRD for the RBD-CRD interactions with KD are highlighted by red points.