Figure 1
From: Molecular recognition of RAS/RAF complex at the membrane: Role of RAF cysteine-rich domain
Simulations of membrane-anchored and solvated RAF-CRD. (a) Per-residue α-carbon B-factors (Å2) from five AA simulations of membrane-anchored CRD (left) and five simulations of solvated CRD (right). Low to high B-factor values are colored from blue to red. Gray spheres denote coordinated zinc ions. The three β-strands comprising the core β-sheet structure are labeled 1–3 in the membrane-anchored structure. N- and C-terminal residues, as well as residues that showed significant chemical shift perturbations in NMR experiments (see Fig. 2a) are also labeled. Typical conformational distortions observed in simulations of solvated CRD, particularly in the two hydrophobic loops (top of the structure), are shown. (b) Free energy (kJ/mol) contour map of membrane-anchored configurations of CRD from AA simulations, using as order parameters (i) the distance along the bilayer normal between the COM of both CRD hydrophobic loops and the bilayer COM, and (ii) the angle between a vector defined along β-strand 2 and the bilayer normal (see Supp. Figure 3a).
