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Researchers get a grip on nervous system's receptors
Date:2/7/2011

tions. They identified four distinct conformations in an AMPA receptor bound to a GluA2 agonist (which triggers the receptor response). Other experiments that involved agonist-free AMPA or AMPA bound to mutated glutamate showed an even floppier receptor.

Knowing how cleft positions match up with the function is valuable, said Jayaraman, who hopes to extend the technique to other signaling proteins with the ultimate goal of designing drugs to manipulate proteins implicated in neurological diseases.

"It was a beautiful combination," she said of the experiments. "We had done a lot of work on this protein and figured out the basic things. What was lacking was this one critical aspect. Being able to collaborate with a physical chemist (Landes) who had the tools allowed us to get details about this protein we wouldn't have seen otherwise."

"Physical chemistry, for all of its existence, amounts to coming up with new tricks to be able to calculate things that nature would not have us calculate," Landes said. "I think our true contribution is to be able to analyze this noisy data to get to what's underneath."


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Contact: David Ruth
druth@rice.edu
713-348-6327
Rice University
Source:Eurekalert

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