Function-Related Dynamics in Multi-Spanning Helical Membrane Proteins Revealed by Solution NMR
Koh Takeuchi,
Yutaka Kofuku,
Shunsuke Imai,
Takumi Ueda,
Yuji Tokunaga,
Yuki Toyama,
Yutaro Shiraishi,
Ichio Shimada
Affiliations
Koh Takeuchi
Cellular and Molecular Biotechnology Research Institute, National Institute of Advanced Industrial Science and Technology, Aomi, Koto, Tokyo 135-0064, Japan
Yutaka Kofuku
Graduate School of Pharmaceutical Sciences, The University of Tokyo, Hongo, Bunkyo, Tokyo 113-0033, Japan
Shunsuke Imai
Center for Biosystems Dynamics Research, RIKEN, Suehiro, Tsurumi, Yokohama 230-0045, Japan
Takumi Ueda
Graduate School of Pharmaceutical Sciences, The University of Tokyo, Hongo, Bunkyo, Tokyo 113-0033, Japan
Yuji Tokunaga
Cellular and Molecular Biotechnology Research Institute, National Institute of Advanced Industrial Science and Technology, Aomi, Koto, Tokyo 135-0064, Japan
Yuki Toyama
Graduate School of Pharmaceutical Sciences, The University of Tokyo, Hongo, Bunkyo, Tokyo 113-0033, Japan
Yutaro Shiraishi
Center for Biosystems Dynamics Research, RIKEN, Suehiro, Tsurumi, Yokohama 230-0045, Japan
Ichio Shimada
Graduate School of Pharmaceutical Sciences, The University of Tokyo, Hongo, Bunkyo, Tokyo 113-0033, Japan
A primary biological function of multi-spanning membrane proteins is to transfer information and/or materials through a membrane by changing their conformations. Therefore, particular dynamics of the membrane proteins are tightly associated with their function. The semi-atomic resolution dynamics information revealed by NMR is able to discriminate function-related dynamics from random fluctuations. This review will discuss several studies in which quantitative dynamics information by solution NMR has contributed to revealing the structural basis of the function of multi-spanning membrane proteins, such as ion channels, GPCRs, and transporters.
