Protein conformational heterogeneity changes upon ligand binding are influenced by ligand properties and can modulate the free energy of binding.

Commonly used covalent PPARγ inhibitors weaken, but do not block, binding of other ligands via an allosteric mechanism where ligands clash with a covalent ligand-induced transcriptionally repressive structural conformation.

The atomic resolution cryo-EM structure of somatostatin receptor 2 (SSTR2) provides insights into the mechanism by which SSTRs recognize their ligands and will serve as a platform to develop selective agonists and therapeutics.

Synthetic PPARγ ligands push and cobind with natural endogenous ligands, instead of compete and displace, which synergistically affects the structure and function of PPARγ.

A combination of molecular dynamics simulations and electron cryomicroscopy characterizes interactions of a pentameric ligand-gated ion channel with 25 lipid molecules, specifically in a functional state in which they were not previously observed.

Detailed structural analysis of NPAS1-ARNT and NPAS3-ARNT complexes, and further comparisons with other bHLH-PAS protein structures, show that this family of mammalian transcription factors have distinct ligand-binding pockets within their molecular architectures.

Binding of a charged small molecule to a membrane protein changes the amplitude of the apparent membrane capacitance by changing the charge density at the surfaces of the membrane.

High-resolution structures of human TRPM2 in different functional states provided the mechanism underlying ligand recognition, channel activation and inhibition.

Effective antiestrogens engage a new structural interaction to improve therapeutic antagonism in hormone-resistant breast cancer cells expressing Y537S estrogen receptor alpha.

A receptor for vascular endothelial growth factor forms dimers in the absence of its ligand, and ligand-binding leads to structural changes that result in increased kinase phosphorylation.