- 一般社団法人 日本生物物理学会
- 生物物理 (ISSN:05824052)
- vol.54, no.3, pp.133-139, 2014 (Released:2014-05-27)
Molecular motor kinesins move processively along microtubules by using energy derived from ATP hydrolysis. Almost all of the intermediate structures of this ATPase reaction cycle have been solved for the monomeric kinesin KIF1A. Based on this structural information, we present here the common atomic mechanisms of kinesin motility, which can be applied not only to the monomeric kinesins but also to the dimeric kinesins. Structural studies have suggested that kinesins accomplish their mission by utilizing the evolutionary conserved strategy among the various ATPases/GTPases/kinases in which they use the energy from the ATP/GTP hydrolysis to attach/detach to/from their effectors.