Extended Data Fig. 1: ATP analog interacts intimately with and stabilizes monomers of BRAF and CRAF kinase domains.
From: Negative regulation of RAF kinase activity by ATP is overcome by 14-3-3-induced dimerization
a, SDS-PAGE gels from SEC traces in Fig. 1a. b, Size exclusion chromatography traces (left) showing CRAFKD-MEK1 complex alone (blue), in the presence of ACP (red) and in the presence of GDC-0879, a RAF dimer promoter (magenta). SDS-PAGE analysis of size exclusion experiments (right). The positions of CRAF and MEK1 are labeled to the right of each gel. Elution volumes at top correspond to all gels. c, BRAF-ACP key interactions diagram. d, BRAF-ACP interaction with key residues highlighted. Blue mesh represents electron density of ACP bound to BRAF, 2Fo-Fc map contoured at 2 σ.
