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The structural arrangement and dynamics of the heteromeric GluK2/GluK5 kainate receptor as determined by smFRET.

08:00 EDT 10th June 2019 | BioPortfolio

Summary of "The structural arrangement and dynamics of the heteromeric GluK2/GluK5 kainate receptor as determined by smFRET."

Kainate receptors, which are glutamate activated excitatory neurotransmitter receptors, predominantly exist as heteromers of GluK2 and GluK5 subunits in the mammalian central nervous system. There are currently no structures of the full-length heteromeric kainate receptors. Here, we have used single molecule FRET to determine the specific arrangement of the GluK2 and GluK5 subunits within the dimer of dimers configuration in a full-length receptor. Additionally, we have also studied the dynamics and conformational heterogeneity of the amino-terminal and agonist-binding domain interfaces associated with the resting and desensitized states of the full-length heteromeric kainate receptor using FRET-based methods. The smFRET data are compared to similar experiments on the homomeric kainate receptor to provide insight into role of the differences in the conformational dynamics between the two to the functional differences. This article is part of a Special Issue entitled: Molecular biophysics of membranes and membrane proteins.

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Name: Biochimica et biophysica acta. Biomembranes
ISSN: 1879-2642
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