The structural arrangement at intersubunit interfaces in homomeric kainate receptors.

ABSTRACT: Kainate receptors are glutamate-gated cation-selective channels involved in excitatory synaptic signaling and are known to be modulated by ions. Prior functional and structural studies suggest that the dimer interface at the agonist-binding domain plays a key role in activation, desensitization, and ion modulation in kainate receptors. Here we have used fluorescence-based methods to investigate the changes and conformational heterogeneity at these interfaces associated with the resting, antagonist-bound, active, desensitized, and ion-modulated states of the receptor. These studies show that in the presence of Na⁺ ions the interfaces exist primarily in the coupled state in the apo, antagonist-bound and activated (open channel) states. Under desensitizing conditions, the largely d

SUBMITTER: Litwin DB 

PROVIDER: S-EPMC6502836 | biostudies-literature | 2019 May

REPOSITORIES: biostudies-literature