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Protein-regulated kainate-type glutamate receptor structure revealed |
The structure of the GluK2-NETO2 complex
.
Photo courtesy of Nanjing UniversityThe structure of the GluK2-NETO2 complex
The extracellular interaction between GluK2 and NETO2
.
Photo courtesy of Nanjing UniversityThe extracellular interaction between GluK2 and NETO2
GluK2's ion-conducting hole and modulation mechanism of internal rectification
.
Photo courtesy of Nanjing University Photo courtesy of Nanjing University
The structure of the desensitized GluK2-NETO2 complex
.
Photo courtesy of Nanjing UniversityThe structure of the desensitized GluK2-NETO2 complex
The research team found that the extracellular domain of NETO2 has a wide range of binding surfaces with kainate receptors
.
By revealing the complex binding patterns of NETO2 and GluK2 receptor amino terminal domains (ATD) and ligand binding domains (LBD), clarified how NETO2 regulates receptor gating dynamics
Neurotransmitters are specific chemicals that act as "messengers" in synaptic transmission and play a very important role in maintaining the body's normal physiological functions
.
Among them, glutamate is the excitatory neurotransmitter with the highest content and the most widespread distribution in the central nervous system.
The kainate receptor (KAR) is a type of ionotropic glutamate receptor, activated by the neurotransmitter glutamate
.
They are not only located at the postsynapse to mediate excitatory neurotransmission in many brain regions, but also appear at the presynapse to regulate the release of excitatory and inhibitory transmitters on the synapse
More specifically, NETO2 modulates KAR gating by slowing down inactivation and desensitization, accelerating recovery from desensitization, and reducing the polyamine blockade of calcium-permeable KAR
.
Although recent progress has been made in the structural research of isolated KARs, the molecular basis of the regulation of NETO protein is still unclear
This study demonstrated the structure of the GluK2-NETO2 complex in the closed state of antagonist binding and the desensitized state of agonist binding, and explained the interaction and stoichiometry between GluK2 and NETO2, as well as the gating and pore characteristics of NETO2 on the GluK2 receptor The adjustment mechanism
.
In addition, the structure of the study provides a more complete pore domain, including the detailed structure of the selective filter
.
The research results provide new enlightenment and new perspectives for understanding excitotoxicity and degenerative neuropathy
.
(Source: Fei Wen Cai, China Science News)
Related paper information: https://doi.
org/10.
1038/s41586-021-03936-y
org/10.
1038/s41586-021-03936-y