Introduction of Session 8, “Structural mechanism of animal rhodopsins and GPCR”
Author:
Affiliation:
1. Department of Chemistry, Graduate School of Science, Chiba University
Publisher
Biophysical Society of Japan
Subject
Physiology,Molecular Biology,Biophysics,Biochemistry,Biochemistry, Genetics and Molecular Biology (miscellaneous)
Link
https://www.jstage.jst.go.jp/article/biophysico/20/Supplemental/20_e201015/_pdf
Reference5 articles.
1. [1] Kishi, K., Kim, Y. S., Fukuda, M., Inoue, M., Kusakizako, T., Wang, P. Y., et al. Structural basis for channel conduction in the pump-like channelrhodopsin ChRmine. Cell 185, 672–689 (2022). https://doi.org/10.1016/j.cell.2022.01.007
2. [2] Reichenwaller, J., Liu, B., Balo, A. R., Ou, W., Ernst, O. P. Electron paramagnetic resonance spectroscopy on G-protein-coupled receptors: Adopting strategies from related model systems. Curr. Opin. Struct. Biol. 69, 177–186 (2021). https://doi.org/10.1016/j.sbi.2021.06.003
3. [3] Nagata, T., Koyanagi, M., Tsukamoto, H., Mutt, E., Schertler, G. F., Deupi, X., et al. The counterion-retinylidene Schiff base interaction of an invertebrate rhodopsin rearranges upon light activation. Commun. Biol. 2, 180 (2019). https://doi.org/10.1038/s42003-019-0409-3
4. [4] Katayama, K., Nonaka, Y., Tsutsui, K., Imai, H., Kandori, H. Spectral tuning mechanism of primate blue-sensitive visual pigment elucidated by FTIR spectroscopy. Sci. Rep. 7, 4904 (2017). https://doi.org/10.1038/s41598-017-05177-4
5. [5] Gruhl, T., Weinert, T., Rodrigues, M., Milne, C. J., Ortolani, G., Nass, K., et al. Ultrafast structural changes direct the first molecular events of vision. bioRxiv (2022). https://doi.org/10.1101/2022.10.14.511948
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