Highlights•Prediction and characterization of allosteric sites.•Protein dynamics is the basis of
allosteric communication.•Theoretical models, experimental verification, and challenges in …

Two competing and mutually exclusive mechanisms of ligand recognition–conformational
selection and induced fit–have dominated our interpretation of ligand binding in biological …

Orthosteric drugs block the active site to obstruct function; allosteric drugs modify the
population of the active state, to modulate function. Available data lead us to propose that …

Protein kinase A (PKA) is a prototype of multidomain signaling proteins functioning as
allosteric conformational switches. Allosteric transitions have been the subject of extensive …

The omnipresence of allosteric regulation together with the fundamental role of structural
dynamics in this phenomenon have initiated a great interest to the detection of regulatory …

Ligand-induced protein allostery plays a central role in modulating cellular signalling
pathways. Here using the conserved cyclic nucleotide-binding domain of protein kinase A's …

The last five years have witnessed major developments in the understanding of the allosteric
phenomenon, broadly defined as coupling between remote molecular sites. Such advances …

Hyperpolarization-activated cyclic nucleotide-gated (HCN) ion channels control neuronal
and cardiac electrical rhythmicity. There are four homologous isoforms (HCN1–4) sharing a …

Allostery is an essential regulatory mechanism of biological function. Allosteric sites are also
pharmacologically relevant as they are often targeted with higher selectivity than orthosteric …

Type II isoforms of cyclic adenosine monophosphate (cAMP)–dependent protein kinase A
(PKA-II) contain a phosphorylatable epitope within the inhibitory domain of RII subunits …