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CSHL structural biologists reveal novel drug binding site in NMDA receptor subunit
Date:6/16/2011

receptors. The results were obtained through biochemistry and x-ray crystallography, a method that features exposing a crystalline form of the molecule under study to very high-energy x-ray beams, which reveals its features in great detail. This enabled the team to demonstrate that phenylethanolamine is recognized at the interface of the GluN1 and GluN2B subunits of the receptor, rather than at a previously predicted site within GluN2B.

"Before this study, we did not have a sufficiently precise map of NMDA receptor subunits to facilitate the design of better and more effective compounds that could dock at the allosteric site. Our results should move drug development in the right direction. We are now optimistic that the field can determine optimal ways of targeting NMDA receptors for therapeutic purposes," Furukawa says.


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Contact: Peter Tarr
tarr@cshl.edu
516-367-5055
Cold Spring Harbor Laboratory
Source:Eurekalert

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