Luminescence resonance energy transfer investigation of conformational changes in the ligand binding domain of a kainate receptor.

ABSTRACT: The apo state structure of the isolated ligand binding domain of the GluR6 subunit and the conformational changes induced by agonist binding to this protein have been investigated by luminescence resonance energy transfer (LRET) measurements. The LRET-based distances show that agonist binding induces cleft closure, and the extent of cleft closure is proportional to the extent of activation over a wide range of activations, thus establishing that the cleft closure conformational change is one of the mechanisms by which the agonist mediates receptor activation. The LRET distances also provide insight into the apo state structure, for which there is currently no crystal structure available. The distance change between the glutamate-bound state and the apo state is similar to that observed bet

SUBMITTER: Du M 

PROVIDER: S-EPMC2556009 | biostudies-literature | 2008 Oct

REPOSITORIES: biostudies-literature