A Finnish-Swiss team cracks the atomic structure of a major cancer drug target

Finnish and Swiss researchers 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 to inhibit 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. Professor Kari Alitalo's research group at the University of Helsinki 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, tells Dr. Veli-Matti Leppänen.

The work was made possible by the long-standing interest and collaborative research of the binational team and the availability of excellent crystallography beamlines at the Swiss Synchrotron Light Source located at PSI, and it was supported by the European Union.

Text: Päivi Leppänen
Picture: Research group

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