Ligand photo-isomerization triggers conformational changes in iGluR2 ligand binding domain.

ABSTRACT: Neurological glutamate receptors bind a variety of artificial ligands, both agonistic and antagonistic, in addition to glutamate. Studying their small molecule binding properties increases our understanding of the central nervous system and a variety of associated pathologies. The large, oligomeric multidomain membrane protein contains a large and flexible ligand binding domains which undergoes large conformational changes upon binding different ligands. A recent application of glutamate receptors is their activation or inhibition via photo-switchable ligands, making them key systems in the emerging field of optochemical genetics. In this work, we present a theoretical study on the binding mode and complex stability of a novel photo-switchable ligand, ATA-3, which reversibly binds to gluta

SUBMITTER: Wolter T 

PROVIDER: S-EPMC3979659 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature