Structure-function analysis reveals an allosteric mechanism activating a plant immune receptor kinase complex.

An integrative structural biology approach provides refined models of the KCNQ1-KCNE1 channel complex, which propose a new mechanism to explain how KCNE1 modulates KCNQ1 channel activation.

Conformation-specific nanobodies enable to capture and solve the first GTP-bound active structure of a bacterial homolog of the Parkinson-associated LRRK2 protein, providing insights into the activation mechanism of these proteins.

Internal dynamics play a crucial functional role in MarR (multiple antibiotic resistance repressor) proteins and their role reconciles the distinct allosteric mechanisms proposed previously.

Aurora A kinase, an anti-cancer drug target, can be activated by two independent mechanisms.

Deciphering the dynamics of the allosteric communication and the formation of transient pockets along the activation pathway of G-protein-coupled receptors provides useful information for the design of allosteric modulators.

A pentameric channel-receptor was studied by combining allosteric mutations, electrophysiology, fluorescent reporters and normal mode analysis, to dissect the long-range allosteric couplings specifically involved in its pre-activation and activation.

An entropy switch controls the Aurora B autoactivation process through two distinct kinetic steps of phosphorylation.

Simulations of molecular dynamics suggest how the binding of the β-grasp domain of SUMO1 induces conformational and dynamic effects to activate SENP1.

Specific residues within an enzyme integrate allosteric inputs that originate from distinct ligand-binding pockets.