Allosteric modulation in the M2 muscarinic receptor derives from a mix of interactions within and between the protomers of an oligomer.

Cholesterol exhibits transient interaction with A2AR and regulates receptor conformational equilibria through indirect membrane effects.

Structural biology studies reveal the importance of protein dynamics on understanding molecular mechanisms underlying allosteric modulation of G protein-coupled receptors (GPCR) that offer insights into future GPCR research and drug discovery.

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.

A series of novel compounds selective for N-methyl-D-aspartate-type glutamate receptor includes positive and negative allosteric modulators that act at the same site, show use-dependence, increase agonist potency, and have differential activity based on the agonist concentration.

Genetically induced conformational modulation of eIF2B activates the Integrated Stress Response by impairing nucleotide exchange.

Localized drug photoactivation provides light-mediated analgesia in behaving mice.

Single molecule subunit counting, FRET and electrophysiology experiments reveal that metabotropic glutamate receptor subunits interact and rearrange at the level of the transmembrane domains in response to allosteric modulators.

A combination of single-molecule and in vivo FRET showed how drugs affect conformation of mGluR2 at different domains.

Development of nanobodies against a model pentameric ligand-gated ion channel demonstrates they can be functionally active as negative or positive allosteric modulators and offers opportunities for future drug development.