NEW YORK, December 18, 2001 – Research published in this week’s issue of Nature describes the molecular structure of two cancer-related proteins binding to one another. Scientists identified the biochemical and signaling properties of these molecules using a process called X-ray crystallography. The technique yielded the first-ever detailed pictures of the proteins interacting with each other, indicating which areas are most essential for the development of cancer. The characterization of the structure may eventually be used to design novel drugs that interfere with the normal function of these proteins and prevent cancer growth. The work is the result of a scientific collaboration led by Memorial Sloan-Kettering Cancer Center. Tyrosine kinases are key enzymes responsible for communication between receptors on the cell’s surface and pathways within the cell. Researchers determined the structure of an Eph receptor tyrosine kinase bound to its corresponding ligand molecule called ephrin. Interactions between Eph receptors and their specific ephrins lead to an array of cellular processes, including those that regulate cell proliferation, survival, adhesion, and movement. They are especially important in angiogenesis – the development of new blood vessels essential for the progression of cancer.
The above story is based on materials provided by Memorial Sloan-Kettering Cancer Center. Note: Materials may be edited for content and length.
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