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Molecular motion in detail: Scientists' high-res images illuminate binding process

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In a critical breakthrough in unraveling how molecular "motors" ferry proteins and nutrients through cells, Harvard scientists have produced high-resolution images that show how the "foot" of dynein—one of the most complex, but least understood such motors—binds to microtubules, the cellular tracks it travels on.

As described in a Sept. 20 paper in Science, a team of researchers, led by Andres Leschziner, associate professor of molecular and cellular biology at Harvard Medical School (HMS), and Samara Reck-Peterson, HMS assistant professor of cell biology, showed that dynein's foot dramatically changes shape as it binds to the microtubule. Those chemical changes, Leschziner said, suggest that the foot acts as a sensor to aid coordinated movement.

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