Synapse-associated protein 97. The model shows the PDZ domain of the SAP97 protein in a ribbon format, highlighting its structural elements. The intra-cellular portion of the NMDA receptor is shown as ball-and-stick format atoms. SAP97 is a scaffolding protein, facilitating nerve signals.
Brown University biologists have solved the structure of a critical piece of synapse-associated protein 97 (SAP97) found in abundance in the heart and head, where it is believed to play a role in everything from cardiac contractions to memory creation. Results are published in The Journal of Biological Chemistry.
Dale Mierke, associate professor of medical science at Brown, said that knowing how a piece of SAP97 is built is an important step. Now that part of the protein’s structure is solved, scientists can create a molecule to disable it. That, in turn, will allow them to fully understand SAP97’s role in the body. And that will point drug makers to targets for developing new ways to treat cardiac or neurological diseases.
"To arrive at a solution, you need to understand the problem,” Mierke said. “Solving protein structures opens doors for effective treatments.”
Wendy Lawton | EurekAlert!
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