By identifying the structure at the atomic level, scientists can now pinpoint where drugs may interact with the protein.
"Many other scientists have studied this protein, but what exactly it is doing has been very difficult to determine," said Shelagh Ferguson-Miller, professor of biochemistry and molecular biology at the Michigan State University in the US.
"Drugs and other compounds bind to TSPO, but without knowing the structure, their effects are hard to interpret. Now that we have obtained the structure, it could provide important clues regarding anxiety disorders and the basis for a new generation of anti-anxiety drugs," Miller added.
TSPO plays a key role in shuttling cholesterol into mitochondria, the cells' powerhouse where the cholesterol is converted to hormones.
These hormones are essential for our body functions.
Using X-ray technology, the team was able to solve the crystal structure of the protein - creating an image of TSPO at a molecular level.
This gave researchers a better understanding on how TSPO interacts with cholesterol and how this relationship affects the creation of steroid hormones.
"One reason that TSPO's function has been so hard to pin down is that many studies have been done in the complex and diverse environments of whole cells and tissues, where a clear-cut interpretation of the results is difficult," said Fei Li, a researcher and co-author from the Michigan State University.
"We were able to obtain a pure protein that was still functional, but isolated from these complications," Fei Li added.
The study appeared in the journal Science.
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