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How molecular motors like Kinesin regulates the affinity to the rail proteinin the process of ATP hydrolysis remains to be uncovered. To understand theregulation mechanism, we investigate the structural fluctuation of KIF1A indifferent nucleotide states that are realized in the ATP hydrolysis process bymolecular dynamics simulations of Go-like model. We found that "alpha4 helix",which is a part of the microtubule (MT) binding site, changes its fluctuationsystematically according to the nucleotide states. In particular, the frequencyof large fluctuations of alpha4 strongly correlates with the affinity of KIF1Afor microtubule. We also show how the strength of the thermal fluctuation andthe interaction with the nucleotide affect the dynamics of microtubule bindingsite. These results suggest that KIF1A regulates the affinity to MT by changingthe flexibility of alpha4 helix according to the nucleotide states.

Structural Fluctuations of Microtubule Binding Site of KIF1A in Different Nucleotide States