Health
Scientists capture 'twisting' movement of NMDAR protein, key to brain signaling
Proteins are constantly doing a kind of dance: they move and they twist. their The body is working to perform certain functions in the body. The NMDAR protein performs a particularly intense dance routine in the brain. One wrong move can lead to a variety of neurological disorders. NMDAR binds to the neurotransmitter glutamate and another compound. glycineThese bonds control the NMDAR's dance step: when the routine is finished, the NMDAR opens. This open ion channel generates an electrical signal that's important for cognitive functions like memory.
The problem is, until now, scientists have been unable to figure out the final step in the NMDAR routine. Now, Professor Hiro Furukawa of Cold Spring Harbor Laboratory and his team have decoded the key dance move that allows the NMDAR to rotate into an open formation. In other words, they've mastered the NMDAR “twist.”
To capture this critical step, Furukawa and his team used a technique called electron microscopy (cryo-EM), which freezes and visualizes proteins. First, the team needed to find a way to keep a type of NMDAR, called GluN1-2B, open long enough to be imaged. So Furukawa teamed up with Professors Steven Treinellis and Dennis Liotta at Emory University. Together, they discovered a molecule that keeps NMDARs open.
“It's not the most stable structure. The NMDAR has a lot of independently moving parts. They have to work together. Everything has to work perfectly for the ion channel to open. Proper behavior and cognition require precise amounts of electrical signals at the right time.”
Professor Hiroyuki Furukawa, Cold Spring Harbor Laboratory
Cryo-EM imaging allows researchers to see exactly how the atoms in NMDARs move as they “twist.” This could one day lead to drug compounds that can teach the lagging NMDARs the correct movement. Better drugs that target NMDARs could have applications in neurological disorders such as Alzheimer's and depression.
“The compounds bind to pockets in the protein, but imperfectly at first. This will enable us, and chemists, to find ways to fill those pockets more perfectly, which will improve the efficacy of the drug. Also, the shape of the pocket is unique. But there could be similarly shaped ones in other proteins, which could cause side effects. So specificity is key,” Furukawa explains.
In fact, there are many types of NMDARs in the brain. Another recent study from the Furukawa lab observed GluN1-3A NMDARs for the first time. Surprisingly, their dance moves are quite different: This routine produces an unusual pattern of electrical signals.
So now you've mastered the twist, now it's time for the head spin.
sauce:
Journal References:
Chou, T.-H. other(2024). Molecular mechanisms of ligand gating and gating of NMDA receptors. Nature. doi.org/10.1038/s41586-024-07742-0.
Michalski, K., & Furukawa, H. (2024). Structure and function of GluN1-3A NMDA receptor-excitatory glycine receptor channels. Scientific advances. doi.org/10.1126/sciadv.adl5952.
Sources 2/ https://www.news-medical.net/news/20240801/Scientists-capture-NMDAR-proteins-twist-motion-key-to-brain-signaling.aspx The mention sources can contact us to remove/changing this article |
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