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Investigating role of conformational changes of microtubule in regulating its binding affinity to kinesin by all-atom molecular dynamics simulation.
Shi, Xiao-Xuan; Fu, Yi-Ben; Guo, Si-Kao; Wang, Peng-Ye; Chen, Hong; Xie, Ping.
Afiliação
  • Shi XX; Key Laboratory of Soft Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing, China.
  • Fu YB; School of Material Science and Engineering, Central South University of Forestry and Technology, Changsha, China.
  • Guo SK; Key Laboratory of Soft Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing, China.
  • Wang PY; Key Laboratory of Soft Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing, China.
  • Chen H; Key Laboratory of Soft Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing, China.
  • Xie P; School of Materials Science and Energy Engineering, FoShan University, Guangdong, China.
Proteins ; 86(11): 1127-1139, 2018 11.
Article em En | MEDLINE | ID: mdl-30132979
ABSTRACT
Changes of affinity of kinesin head to microtubule regulated by changes in the nucleotide state are essential to processive movement of kinesin on microtubule. Here, using all-atom molecular dynamics simulations we show that besides the nucleotide state, large conformational changes of microtubule-tubulin heterodimers induced by strong interaction with the head in strongly binding state are also indispensable to regulate the affinity of the head to the tubulin. In strongly binding state the high affinity of the head to microtubule arises largely from mutual conformational changes of the microtubule and head induced by the specific interaction between them via an induced-fit mechanism. Moreover, the ADP-head has a much weaker affinity to the local microtubule-tubulin, whose conformation is largely altered by the interaction with the head in strongly binding state, than to other unperturbed tubulins. This indicates that upon Pi release the ADP-head temporarily has a much weaker affinity to the local tubulin than to other tubulins.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Tubulina (Proteína) / Cinesinas / Simulação de Dinâmica Molecular / Microtúbulos Limite: Animals Idioma: En Ano de publicação: 2018 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Tubulina (Proteína) / Cinesinas / Simulação de Dinâmica Molecular / Microtúbulos Limite: Animals Idioma: En Ano de publicação: 2018 Tipo de documento: Article