HEADLINES Published October23, 2015 By Jerwin Jay Taping

Scientists Finally Know Structure of Key Enzyme Complex Involved In Cancer Development

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Scientist determined the structure of cancer-driving enzyme-complex through x-ray crystallography
(Photo : NASA | Hulton Archive, Getty Images News)

After so many years, US researchers have finally determined the atomic structure of a key enzyme that plays a key role in driving the formation of several types of cancer. PRC2 is the protein that results from a certain gene mutation, and is highly linked to the development of lymphoma, brain cancers, and most especially leukemia.

PRC2, or polycomb repressive complex 2, is an enzyme that regulates gene expressions through modifying the structure of chromatin - a complex containing DNA and protein. Abnormal structure or folding of PRC2 enzyme, which is usually caused by mutations in the PRC2 gene, results to irregular functions that lead to certain diseases, which cancer is but one kind.

"Our findings bring us one step closer to understanding the chemistry of how PRC2 functions in normal cells and how mutations in the gene cause disease," says senior author Dr. Xin Liu, assistant professor of Obstetrics and Gynecology at UT Southwestern, as quoted in the press release.

"Producing either too much of too little PRC2 enzyme can unexpectedly silence or activate genes, which is not good for the cell," Dr. Liu adds.

The study aimed to determine how a normal level of PRC2 enzyme activity is controlled inside the cells, and how the enzyme acts in various ways. Such a goal, however, seemed practically impossible, because the enzyme interacts with numerous proteins in the human body at the same time.   

However, the research team found a new approach to achieve the long-standing objectives. Dr. Liu and his colleagues reproduced a 3D atomic structure of PRC2 crystals through an imaging technique called x-ray crystallography, ScienceAlert writes. To know its structure is very necessary since it is what determines and influence its function. Having that information, researchers will be able to finally understand how the enzyme behaves in normal and diseased cells.

Interestingly, such a work did not only solve some mysteries about the mechanisms of the enzyme in gene regulation, but also provided the structure which if synthetically reproduced can lead to the development of future cancer therapies.

"Indeed, several clinical trials are currently ongoing to target PRC2, and we believe our work will shed light on these and other studies in drug development by offering insights into how PRC2 works at the atomic level," says Dr. Liu.

The study appears in the journal Science.

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