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作 者:耿轶钊 鲁丽爱 贾宁 张冰冰 纪青 Yi-Zhao Geng;Li-Ai Lu;Ning Jia;Bing-Bing Zhang;Qing Ji(School of Science,Hebei University of Technology,Tianjin 300401,China;Institute of Biophysics,Hebei University of Technology,Tianjin 300401,China)
机构地区:[1]School of Science,Hebei University of Technology,Tianjin 300401,China [2]Institute of Biophysics,Hebei University of Technology,Tianjin 300401,China
出 处:《Chinese Physics B》2023年第10期738-748,共11页中国物理B(英文版)
基 金:supported by the Natural Science Foundation of Hebei Province of China(Grant No.A2020202007);the National Natural Science Foundation of China(Grant No.11605038)。
摘 要:Microtubule catalyzes the mechanochemical cycle of kinesin,a kind of molecular motor,through its crucial roles in kinesin's gating,ATPase and force-generation process.These functions of microtubule are realized through the kinesin-microtubule interaction.The binding site of kinesin on the microtubule surface is fixed.For most of the kinesin-family members,the binding site on microtubule is in the groove betweenα-tubulin andβ-tubulin in a protofilament.The mechanism of kinesin searching for the appropriate binding site on microtubule is still unclear.Using the molecular dynamics simulation method,we investigate the interactions between kinesin-1 and the different binding positions on microtubule.The key non-bonded interactions between the motor domain and tubulins in kinesin's different nucleotide-binding states are listed.The differences of the amino-acid sequences betweenα-andβ-tubulins make kinesin-1 binding to theα–βgroove much more favorable than to theβ–αgroove.From these results,a two-step mechanism of kinesin-1 to discriminate the correct binding site on microtubule is proposed.Most of the kinesin-family members have the conserved motor domain and bind to the same site on microtubule,the mechanism may also be shared by other family members of kinesin.
关 键 词:KINESIN TUBULIN MICROTUBULE molecular dynamics simulation
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