「Biophysics and Physicobiology」にKei Moritsugu et al. “Allosteric response to ligand binding: Molecular dynamics study of the N-terminal domains in IP₃ receptor”を掲載

2019年11月29日 学会誌

日本生物物理学会欧文誌［Biophysics and Physicobiology］に以下の論文が新規掲載されました。

Kei Moritsugu, Tsubasa Ito, Akinori Kidera “Allosteric response to ligand binding: Molecular dynamics study of the N-terminal domains in IP₃ receptor”

【Significance】
Allosteric structural change of IP₃ receptor

Allostery has long been a key concept of biomolecular physics in the context of molecular function. Here, we simulated the allosteric structural change of IBC/SD domains in IP₃R and found the response upon IP3 binding appearing in two different modes: one with a collective motion within a linear response regime and the other with an overamplified motion beyond the linear regime. The domain and subunit arrangement in IP₃R is designed to maintain collective and linear dynamics, which enables the large-scale allosteric communication from the IP3 binding site to the ion channel gate in IP₃R.

Biophysics and Physicobiology, Vol.16, 232-239


URL:https://doi.org/10.2142/biophysico.16.0_232

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