(locked-down kinesin motor heads in yellow and orange, with tail domain in blue)DAVID HACKNEY
H.Y. Kaan et al., “The structure of the kinesin-1 motor-tail complex reveals the mechanism of autoinhibition,” Science, 333:883-85, 2011.
In a major advance of work that he began 11 years ago, Frank Kozielski, at the Beatson Institute for Cancer Research in Glasgow, revealed a critical component of the structure of kinesin-1—a motor protein involved in shuttling cargo throughout the cell. The structure helped settle a debate about how the molecule stays inactive until it has cargo to transport.
Researchers knew that kinesin would halt when the tail domains—with their two motor heads that walk along the microtubules—were not attached to cargo, but they didn’t know how. Some researchers proposed that the tail would change the shape of the motor so it could not function; others ...
