Kinesins:microtubule Kinesins microtubule Kinesins bind microtubules All kinesins contain a motor domain or head, the position varies but it is structurally highly conserved (Kull et al. 1996, Sablin et al. 1996). The microtubule-binding site includes structural elements which interact with tubulin and undergo movement between the ADP and ATP bound states. The highly conserved switch I (SSRSH) and II (DLAGSE) motifs, which change in conformation during the ATP hydrolysis cycle, form a salt-bridge that, in myosin, closes the nucleotide-binding cleft, enabling the motor to hydrolyze ATP (Geeves & Holmes 1999). This closed conformation has now been seen in a crystal structure of the frog kinesin-5 Eg5 (Parke et al. 2010). Authored: Akkerman, JW, 2010-10-29 Edited: Jupe, S, 2010-11-15 Pubmed10872464 Pubmed15326200 Pubmed1607388 Pubmed16262723 Pubmed19116309 Pubmed20018897 Pubmed2521221 Pubmed2522352 Pubmed7929562 Pubmed8606779 Pubmed8606780 Reactome Database ID Release 43983266 Reactome, http://www.reactome.org ReactomeREACT_25309 Reviewed: Ouwehand, WH, 2010-11-12