According to the American Physicists Organization Network report, cancer researchers at the University of California, Santa Cruz recently observed the molecular mechanism of biochemical reactions in cells, explaining how tumor suppressor genes control the cell growth and division cycle, which helps to develop new approaches to cancer treatment . The research was published in "Natural Structure and Molecular Biology".
At present, it is known that the eye cancer tumor suppressor gene protein is like a door. Whether it opens or closes controls the growth and division of cells. Adding or removing phosphate groups in the protein chain can regulate the cell growth cycle. An activating enzyme called a cell cycle-dependent protein has a phosphate group added to it, and the door to growth is opened, and the cell begins to divide; another enzyme called protein phosphate 1 is responsible for removing the phosphate group. The door closed. In many types of cancer, if the door is kept open, the cells will multiply and lose control.
Seth Rubin, associate professor of chemistry and biochemistry at the University of California, Santa Cruz, said: "From an internal mechanism level to understand the operation of proteins, we can successfully target them with drugs. The easiest way is to use drugs to disable this protein, But we also need it to be opened or closed at an appropriate time. "
Rubin ’s team used crystal X-ray diffraction to draw a three-dimensional structure of the eye cancer protein that binds to phosphatase, and found that when the phosphatase binds to the protein, the door is closed, but in the same position. When combined with an activating enzyme, it will add a phosphate group to open the door. The two enzymes are competing for the same "parking space" to control the door.
Experiments show that activating enzyme and phosphatase are indeed competing in the same fixed position to perform their respective tasks. The researchers used this competition to cultivate eye cancer protein cells with specific growth and division patterns. They used a mutated phosphatase, which is unable to perform the normal phosphate-clearing work, which shows that as long as it is combined with eye cancer protein, it can lock the activated enzyme. The research team also worked with Canadian cancer researchers to conduct experiments in living cells.
"This explains how to bind the phosphatase, so that it can not only clear the phosphate group and close the door, but also lock the 'parking space' so that the activated enzyme can't get close, so that the door can be closed for a long time." Rubin said. Activating enzymes are key targets in drug development. Understanding the competitive role between activating enzymes and phosphatases can help guide the direction of drug development. "
Protein structure shows opening and closing of tumor suppressor genes
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