X-ray crystallography approach could halt spread of tumor cells

Researchers from the Department of Chemistry and Molecular Biology at the University of Gothenburg (Göteborg, Sweden) have managed for the first time to obtain detailed information about the role of the protein metastasin in the spread of tumor cells. Obtained using x-ray crystallography, the work could lead to better drug development.

Previous research has shown that metastasin is activated through the binding of calcium ions, and then binds to and modulates other proteins. One of metastasin’s binding partners is a motor protein called non-muscle myosin. Motor proteins are the driving force behind cell mobility. By binding to this protein, metastasin can increase the spread of tumor cells, acting as a "gas pedal" for the cancer engine.

It has been possible to image metastasin and calcium-ion-bound metastasin using x-ray crystallography before, but the University of Gothenburg researchers—led by Gergely Katona—are the first to have imaged the structure of calcium-ion-activated metastasin with an attached non-muscle myosin fragment. The discovery gave them information about regions of both metastasin and the motor protein that are crucial for metastasin’s ability to bind to the motor protein, which could yield development of drugs that block these specific regions and prevent this binding.

The metastasin and the motor protein can be imaged as a snapshot, but the next stage is to create a video to see how the molecules move when binding to one another, explains Katona.

The work was published recently in the Proceedings of the National Academy of Sciences (PNAS); for more information, please visit http://www.pnas.org/content/early/2012/03/27/1114732109.abstract?sid=f7ab6edc-51c7-4b2a-b884-a6e841c3ea31.

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