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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 1. B-Raf autoinhibition in the presence of the 14-3-3 dimer.

Figure 1.

(A) B-Raf consists of the N-terminal RBD-CRD and C-terminal kinase domain (KD). The phosphorylated sites in the middle loop (pSer365) and C-terminal tail (pSer729) interact with the 14-3-3 dimer. The release of pSer365 and RBD-CRD activates B-Raf.

(B–D) (B) The structures of the fully autoinhibited B-Raf in complex with the 14-3-3 dimer. The (C) pSer365 and (D) pSer729 form strong interactions with the basic residues (K49, R56, R127) in 14-3-3 dimer.