MCB 2210 Lecture Notes - Lecture 15: Processivity, Atp Hydrolysis, Kinesin
1 Nov 2016
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Document Summary
Three kinesin classes: differ in the location of the motor domain in the primary sequence of the protein, kin-n kinesins. Have the motor domain at the n-terminus of the protein. Kin-n move towards the microtubule (+) plus ends: kin-c kinesins. Kin-c kinesins move towards the (-) minus ends. These kinesins are rare: kin-i kinesins. Have an internal motor domain (centrally located in the protein sequence) Kin-i kinesins do not move along microtubules but bind microtubule ends and promote protofilament peeling. Kinesin differ in organization and function: conventional kinesin was the first kinesin discovered and is the best characterized. Microtubule gliding assay: the motor function of kinesin can be directly demonstrated by microscopic gliding assays. Kinesin cross-bridge cycle: kinesins undergo cross-bridge cycle similar to that of myosins in which atp hydrolysis and pi release are coupled to conformational changes in the head and neck domains of the molecule.
