Structural Arrangement Produced by Concanavalin A Binding to Homomeric GluK2 Receptors.

ABSTRACT: Kainate receptors are members of the ionotropic glutamate receptor family. They form cation-specific transmembrane channels upon binding glutamate that desensitize in the continued presence of agonists. Concanavalin A (Con-A), a lectin, stabilizes the active open-channel state of the kainate receptor and reduces the extent of desensitization. In this study, we used single-molecule fluorescence resonance energy transfer (smFRET) to investigate the conformational changes underlying kainate receptor modulation by Con-A. These studies showed that Con-A binding to GluK2 homomeric kainate receptors resulted in closer proximity of the subunits at the dimer-dimer interface at the amino-terminal domain as well as between the subunits at the dimer interface at the agonist-binding domain. Additionall

SUBMITTER: Gonzalez CU 

PROVIDER: S-EPMC8401665 | biostudies-literature | 2021 Aug

REPOSITORIES: biostudies-literature