PDZ domains are highly abundant protein–protein interaction modules and are often found
in multidomain scaffold proteins. PDZ-domain-containing scaffold proteins regulate multiple …

The PDZ domain is a protein–protein interacting module that plays an important role in the
organization of signaling complexes. The recognition of short intrinsically disordered C …

The canonical binding mode of PDZ domains to target motifs involves a small interface,
unlikely to fully account for PDZ-target interaction specificities. Here, we review recent work …

Allosteric effect implies ligand binding at one site leading to structural and/or dynamical
changes at a distant site. PDZ domains are classic examples of dynamic allostery without …

Abstract Post-synaptic density-95, disks-large and zonula occludens-1 (PDZ) domains are
small globular protein–protein interaction domains widely conserved from yeast to humans …

While allostery is of paramount importance for protein signaling and regulation, the
underlying dynamical process of allosteric communication is not well understood. The PDZ3 …

Dishevelled (DVL) is the key component of the Wnt signaling pathway. Currently, DVL
conformational dynamics under native conditions is unknown. To overcome this limitation …

We have captured the binding of a peptide to a PDZ domain by unbiased molecular
dynamics simulations. Analysis of the trajectories reveals on-pathway encounter complex …

PDZ domain proteins control multiple cellular functions by governing assembly of protein
complexes. It remains unknown why individual PDZ domains can bind the extreme C …

While being a thoroughly studied model of dynamic allostery in a small protein, the pathway
of signal transduction in the PDZ3 domain has not been fully determined. Here, we …