Reference: Kozielski F, et al. (1997) The crystal structure of dimeric kinesin and implications for microtubule-dependent motility. Cell 91(7):985-94

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Abstract


The dimeric form of the kinesin motor and neck domain from rat brain with bound ADP has been solved by X-ray crystallography. The two heads of the dimer are connected via a coiled-coil alpha-helical interaction of their necks. They are broadly similar to one another; differences are most apparent in the head-neck junction and in a moderate reorientation of the neck helices in order to adopt to the coiled-coil conformation. The heads show a rotational symmetry (approximately 120 degrees) about an axis close to that of the coiled-coil. This arrangement is unexpected since it is not compatible with the microtubule lattice. In this arrangement, the two heads of a kinesin dimer could not have equivalent interactions with microtubules.

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Journal Article | Research Support, Non-U.S. Gov't
Authors
Kozielski F, Sack S, Marx A, Thormählen M, Schönbrunn E, Biou V, Thompson A, Mandelkow EM, Mandelkow E
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