神戸大学附属図書館デジタルアーカイブ
入力補助
English
カテゴリ
学内刊行物
ランキング
アクセスランキング
ダウンロードランキング
https://hdl.handle.net/20.500.14094/90006940
このアイテムのアクセス数:
18
件
(
2024-04-25
10:20 集計
)
閲覧可能ファイル
ファイル
フォーマット
サイズ
閲覧回数
説明
90006940 (fulltext)
pdf
10.0 MB
15
メタデータ
ファイル出力
メタデータID
90006940
アクセス権
open access
出版タイプ
Version of Record
タイトル
Affinity of rhodopsin to raft enables the aligned oligomer formation from dimers: Coarse-grained molecular dynamics simulation of disk membranes
著者
Kaneshige, Yukito ; Hayashi, Fumio ; Morigaki, Kenichi ; Tanimoto, Yasushi ; Yamashita, Hayato ; Fujii, Masashi ; Awazu, Akinori
著者名
Kaneshige, Yukito
著者名
Hayashi, Fumio
著者ID
A1236
研究者ID
1000010358179
KUID
https://kuid-rm-web.ofc.kobe-u.ac.jp/search/detail?systemId=f6c039bc884596f8520e17560c007669
著者名
Morigaki, Kenichi
森垣, 憲一
モリガキ, ケンイチ
所属機関名
バイオシグナル総合研究センター
著者名
Tanimoto, Yasushi
著者名
Yamashita, Hayato
著者名
Fujii, Masashi
著者名
Awazu, Akinori
収録物名
PLoS ONE
巻(号)
15(2)
ページ
e0226123-e0226123
出版者
Public Library of Science
刊行日
2020-02-07
公開日
2020-03-24
抄録
The visual photopigment protein rhodopsin (Rh) is a typical G protein-coupled receptor (GPCR) that initiates the phototransduction cascade in retinal disk membrane of rod-photoreceptor cells. Rh molecule has a tendency to form dimer, and the dimer tends to form rows, which is suggested to heighten phototransduction efficiency in single-photon regime. In addition, the dimerization confers Rh an affinity for lipid raft, i.e. raftophilicity. However, the mechanism by which Rh-dimer raftophilicity contributes to the organization of the higher order structure remains unknown. In this study, we performed coarse-grained molecular dynamics simulations of a disk membrane model containing unsaturated lipids, saturated lipids with cholesterol, and Rh-dimers. We described the Rh-dimers by two-dimensional particle populations where the palmitoyl moieties of each Rh exhibits raftophilicity. We simulated the structuring of Rh in a disk for two types of Rh-dimer, i.e., the most and second most stable Rh dimers, which exposes the raftophilic regions at the dimerization-interface (H1/H8 dimer) and two edges away from the interface (H4/H5 dimer), respectively. Our simulations revealed that only the H1/H8 dimer could form a row structure. A small number of raftophilic lipids recruited to and intercalated in a narrow space between H1/H8 dimers stabilize the side-by-side interaction between dimers in a row. Our results implicate that the nano-sized lipid raft domains act as a “glue” to organize the long row structures of Rh-dimers.
カテゴリ
バイオシグナル総合研究センター
学術雑誌論文
権利
© 2020 Kaneshige et al.
This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
詳細を表示
資源タイプ
journal article
言語
English (英語)
eISSN
1932-6203
OPACで所蔵を検索
CiNiiで学外所蔵を検索
関連情報
DOI
https://doi.org/10.1371/journal.pone.0226123
URI
https://www.kobe-u.ac.jp/research_at_kobe/NEWS/news/2020_02_17_01.html
ホームへ戻る