Fig. 2: Structures of the autoinhibited, monomeric BRAF:14-3-32:MEK and BRAF:14-3-32 complexes.
From: Structural insights into the BRAF monomer-to-dimer transition mediated by RAS binding
a Cryo-EM density map at a 3.7 Å resolution (left) and structure of the BRAF:14-3-32:MEK (right) autoinhibited complex. b Cryo-EM density map at a 4.1 Å resolution (left) and structure of the BRAF:14-3-32 (right) autoinhibited complex. Regions of the BRAF monomer and the 14-3-3 dimer are colored as previously described and MEK is shown in gray.
