Fig. 3: Interactions due to the conformational change of the complex formed by DOCK5•ELMO1 and two Rho-GTPases in the extended-open form.
From: Conformational alteration of DOCK5•ELMO1 signalosome on lipid membrane
a Structural models of the closed (PDB: 8JHK) and extended-open forms of the complex superimposed on the DHR-2 domain. Movements of the α-helix (residues 1186–1211) at the C-terminus of the ARM domain, which connects to the DHR-2 domain in DOCK5 and serves as the epicentre of the conformational change, are indicated by red dashed lines. b Conformational change in the region highlighted by the orange box in (a) and its effect on the interaction between DOCK5 and ELMO. The transition to the extended-open form brings the acidic residues D1214 and E1215 in the hinge region of DOCK5 (between the ARM and DHR-2 domains) into close proximity with the basic residues K584 and K607 in the PH domain of ELMO1. c PH domain of ELMO1 oriented toward the lipid membrane in the extended-open form. Basic residues on the VL1 loop of the PH domain are positioned close to the lipid membrane.
