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Scientists solve the structure of a membrane protein that is increased in cancer


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#1 whcaroline

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Posted 22 January 2017 - 08:45 AM

A team led by researchers from University of California, Case Western Reserve University School of Medicine, and ChemoCentryx Inc. has solved the structure of a membrane protein called the atypical chemokine receptor 3 (ACKR3). The study, published online 18 January 2017 in Nature Communications, could facilitate the development of ACKR3 inhibitors.
ACKR3 is able to bind chemokines CXCL11 and CXCL12. ACKR3 is upregulated in many cancer types, making it a potential drug target. Scientists want to slow tumor growth and metastasis by blocking the receptor, but it is not easy to accomplish. The reason is that the structure of the receptor remains elusive.
Lead researcher Tracy M. Handel and the team used several advanced methods, such as X-ray crystallography and mass spectrometry, to investigate the structure of ACKR3, its interaction with an experimental drug for glioblastoma, and its interaction with chemokines. Chemkines are a group of tiny secreted proteins that induce chemotaxis (migration) of target cells. The interactions between chemokines and seven-transmembrane chemokine receptors are known to drive cell migration. Study co-author Mark R. Chance said that "ACKR3 can signal cells to grow and move accelerating their cancer potential."
Finally, the researchers created the first complete structural model for ACKR3, and identified the region in the receptor that interacts with other molecules. These findings will potentially allow for the development of more effective ACKR3 inhibitors. Besides, the method structures of molecules used in the study may also apply to other proteins that contribute to cancer. CusAb (http://www.cusabio.com/) is a manufacturer of proteins and antibodies.





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