PSI scientist Kurt Ballmer-Hofer next to the fermenter in which some of the molecules used for the examination of the development of blood and lymph vessels were produced. (PSI/F. Reiser)
A Finnish-Swiss team cracks the atomic structure of a major cancer drug target - Researchers at Biomedicum Helsinki, Finland, and the Paul Scherrer Institute (PSI) in Villigen, Switzerland, have determined the crystal structure of the ligand-binding domain of a vascular endothelial growth factor (VEGF) receptor in complex with one of its ligands (VEGF-C). Cancer cells require access to blood and lymph vessels for invasive growth and metastasis. By releasing VEGFs, cancer cells stimulate the surrounding blood vessels to invade the cancerous tumor mass. Blocking this process is a new strategy for inhibiting tumor growth. VEGFs and their receptors have been identified as major targets for drug development in cancer therapy, and the VEGF receptor that the groups analyzed is currently the most important target of such drugs. The Finnish group discovered the VEGF-C growth factor in 1996 and found that it is involved in lymphatic vessel growth, cancer metastasis and, more recently, also in blood vessel growth in cancer. The collaborative work published in PNAS by the two research teams provides significant new insights into VEGF receptor function.
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