Solved protein puzzle opens door to new design for cancer drugs
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CORVALLIS, Ore. – Researchers at Oregon State University have solved a longstanding puzzle concerning the design of molecular motors, paving the way toward new cancer therapies.

Findings were published today in Current Biology.

The research involved kinesins: tiny, protein-based motors that interact with microtubules inside cells. The motors convert chemical energy into mechanical energy to generate the directional movements and forces necessary to sustain life.

Microtubules are microscopic tubular structures that have two distinct ends: a fast-growing plus end and a slow-growing minus ends. Microtubules help make up a cell’s skeleton.

Most kinesins only interact with just one microtubule, but a subgroup of kinesins called kinesin-14s preferentially bind to two different microtubules: one with the protein’s feet, and one with its tail.

Scientists had known little about what drives that preference, but researchers in the OSU College of Science revealed that some kinesin-14s have a stiff rather than a flexible waist separating the feet from the tail – that’s the reason these motor proteins prefer a two-microtubule track.

The findings are important because certain cancer cells depend on kinesin-14 to proliferate, and now there’s way to halt those cells: with drugs that make that stiff waist more elastic, thus

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