The main objective of WG1 is to elucidate the protein-protein interactions and dynamics that give rise to signal transduction at the molecular-level, with emphasis on how modulation of these interactions generates specificity in transmembrane receptor-mediated signal transduction. Together with the other work groups, WG1 contributes molecular-level detail to the holistic map of signal transduction developed by the Action.
Specifically, WG1 focuses on the structural basis for molecular interactions among signaling proteins using high-resolution methods (e.g. X-ray crystallography, NMR, cryo-electron microscopy), on the dynamic interactions among signaling proteins using time-resolved methods (e.g. NMR, EPR, single molecule FRET, super-resolution microscopy), and on the analysis of different aspects of these interactions using computational approaches.
Additional goals include identifying key features in protein structure and dynamics that are shared among signaling proteins or those that determine interaction specificity, examining how kinetics of molecular interactions influence signaling, studying the interplay between subcellular localization and protein-protein interactions, or investigating how genetic variations perturb or modulate such interactions.