Figure 2. Interfaces in the FAK oligomeric assembly on the membrane.

1. Close‐up of the central symmetric dimer of the AMP‐PNP particle from the membrane distal view. Interfaces within the symmetric dimer are formed intramolecularly between the FERM and kinase domains (F and K; F’ and K’). Intermolecular interfaces are formed within the symmetric dimer between F and K’, F’ and K as well as K and K’. Intermolecular interactions that link symmetric dimers are formed between two FERM domains (F and F*; F’ and F**). Coloring is as in Fig 1E. The FERM subdomains F1 and F3 (F2 is not visible from this view), kinase N‐ and C‐lobes (K_N, K_C), AMP‐PNP and the N‐ and C‐termini (N, C) are labeled.
2. Superposition of W266‐mediated FERM–FERM 3D‐crystallographic dimers (Ceccarelli et al, 2006) (yellow; PDB: 2AEH) and the FERM–FERM contacts seen in the cryo‐EM structure to link symmetric dimers (F–F*; F’–F**). The view is 90° rotated from panel (A). Subdomains and termini are labeled, and disordered regions in the linker are shown as dashed line.