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タイトル: | Shift in Conformational Equilibrium Induces Constitutive Activity of G-Protein-Coupled Receptor, Rhodopsin |
著者: | Maeda, Ryo Hiroshima, Michio Yamashita, Takahiro Wada, Akimori Sako, Yasushi Shichida, Yoshinori Imamoto, Yasushi https://orcid.org/0000-0002-0803-4163 (unconfirmed) |
著者名の別形: | 山下, 高廣 今元, 泰 |
発行日: | 10-May-2018 |
出版者: | American Chemical Society (ACS) |
誌名: | The Journal of Physical Chemistry B |
巻: | 122 |
号: | 18 |
開始ページ: | 4838 |
終了ページ: | 4843 |
抄録: | Constitutively active mutants (CAMs) of G-protein-coupled receptors (GPCRs) cause various kinds of diseases. Rhodopsin, a light-absorbing GPCR in animal retinas, has retinal as an endogenous ligand; only very low levels of activation of G-protein can be obtained with the ligand-free opsin. However, the CAM of opsin activates G-protein much more efficiently than the wild type, but the mechanism underlying this remains unclear. The present work revisits the constitutive activity of rhodopsin from the standpoint of conformational dynamics. Single-molecule observation of the M257Y mutant of bovine rhodopsin demonstrated that the switch between active and inactive conformations frequently occurred in M257Y opsin, and frequent generation of the active state results in the population shift toward the active state, which accounts for the constitutive activity of M257Y opsin. Our findings demonstrate that the protein function has a direct connection with the structural dynamics. |
著作権等: | This document is the Accepted Manuscript version of a Published Work that appeared in final form in The Journal of Physical Chemistry B, copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see https://doi.org/10.1021/acs.jpcb.8b02819. This is not the published version. Please cite only the published version. この論文は出版社版でありません。引用の際には出版社版をご確認ご利用ください。 |
URI: | http://hdl.handle.net/2433/243174 |
DOI(出版社版): | 10.1021/acs.jpcb.8b02819 |
PubMed ID: | 29668280 |
出現コレクション: | 学術雑誌掲載論文等 |
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