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8TID

Combined linker domain of N-DRC and associated proteins Tetrahymena

これはPDB形式変換不可エントリーです。
8TID の概要
エントリーDOI10.2210/pdb8tid/pdb
EMDBエントリー41284 41376
分子名称Dynein regulatory complex protein 1/2 N-terminal domain-containing protein, Dynein regulatory complex protein 9, Dynein regulatory complex protein 10, ... (24 entities in total)
機能のキーワードnexin-dynein regulatory complex, cilia, axoneme, dynein, structural protein
由来する生物種Tetrahymena thermophila
詳細
タンパク質・核酸の鎖数30
化学式量合計2072904.54
構造登録者
主引用文献Ghanaeian, A.,Majhi, S.,McCafferty, C.L.,Nami, B.,Black, C.S.,Yang, S.K.,Legal, T.,Papoulas, O.,Janowska, M.,Valente-Paterno, M.,Marcotte, E.M.,Wloga, D.,Bui, K.H.
Integrated modeling of the Nexin-dynein regulatory complex reveals its regulatory mechanism.
Nat Commun, 14:5741-5741, 2023
Cited by
PubMed Abstract: Cilia are hairlike protrusions that project from the surface of eukaryotic cells and play key roles in cell signaling and motility. Ciliary motility is regulated by the conserved nexin-dynein regulatory complex (N-DRC), which links adjacent doublet microtubules and regulates and coordinates the activity of outer doublet complexes. Despite its critical role in cilia motility, the assembly and molecular basis of the regulatory mechanism are poorly understood. Here, using cryo-electron microscopy in conjunction with biochemical cross-linking and integrative modeling, we localize 12 DRC subunits in the N-DRC structure of Tetrahymena thermophila. We also find that the CCDC96/113 complex is in close contact with the DRC9/10 in the linker region. In addition, we reveal that the N-DRC is associated with a network of coiled-coil proteins that most likely mediates N-DRC regulatory activity.
PubMed: 37714832
DOI: 10.1038/s41467-023-41480-7
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (3.6 Å)
構造検証レポート
Validation report summary of 8tid
検証レポート(詳細版)ダウンロードをダウンロード

227561

件を2024-11-20に公開中

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