Kinesins monomeric

The monomeric rat kinesin construct (amino acids 1-354) comprises the head domain (including the core motor domain, amino acids 2-325, and the neck linker, amino acids 326-338) and the first half of the neck domain. In the crystal structure, the neck linker consists of two strands, /19 and /110, that form hydrogen bonds with strands />8 and fJ7 of the core /1-sheet (Fig. 2E). The neck linker ends close to loop L10 at the tip of the core domain where the (a-helical neck domain (helix a7) is attached to the core motor domain. Its orientation is roughly in the plane of the core /1-sheet and perpendicular to the strands. 

More than 18 classes of myosin have been identified in different organisms so far. Myosins of class V and class XI (the plant class V) are most akin to kinesin because they are dimeric, plus end (barbed end)-directed, processive motors used for membrane and particle transport along actin filaments. There is also a class of myosins with reversed motility (class VI). It is not yet clear whether these are monomeric or dimeric. Myosin-I, the first class of unconventional myosins to be identified, comprises monomeric motors with a basic tail that interacts by electrostatic interaction with the cargo. 

Hoenger, A., Sack, S., Thormahlen, M., Marx, A., Muller, J., Gross, H., and Mandelkow, E. (1998). Image reconstructions of microtubules decorated with monomeric and dimeric kinesins Comparison with x-ray structure and implications for motility. /. CeU Biol. 141,419-430. 

Kikkawa, M., Okada, Y., and Hirokawa, N. (2000). 15 A resolution model of the monomeric kinesin motor, KIF1A. Cell 100, 241-252. 

Binding Affinity between the Monomeric Kinesin and MT, and the Conformation of Neck-Linker with Varying Nucleotide State... 

Moyer ML, Gilbert SP, Johnson KA. 1998. Pathway of ATP hydrolysis hy monomeric and dimeric kinesin. Biochemistry 37 800. 

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