5Y3A
Crystal structure of Ragulator complex (p18 49-161)
5Y3A の概要
エントリーDOI | 10.2210/pdb5y3a/pdb |
関連するPDBエントリー | 5Y38 5Y39 |
分子名称 | Ragulator complex protein LAMTOR1, Ragulator complex protein LAMTOR2, Ragulator complex protein LAMTOR3, ... (7 entities in total) |
機能のキーワード | ragulator complex, lamtor, signaling protein |
由来する生物種 | Homo sapiens (Human) 詳細 |
細胞内の位置 | Late endosome membrane; Lipid-anchor; Cytoplasmic side: Q6IAA8 Late endosome membrane ; Peripheral membrane protein ; Cytoplasmic side : Q9Y2Q5 Q9UHA4 Lysosome : Q0VGL1 Cytoplasm: O43504 |
タンパク質・核酸の鎖数 | 10 |
化学式量合計 | 121714.51 |
構造登録者 | |
主引用文献 | Zhang, T.,Wang, R.,Wang, Z.,Wang, X.,Wang, F.,Ding, J. Structural basis for Ragulator functioning as a scaffold in membrane-anchoring of Rag GTPases and mTORC1. Nat Commun, 8:1394-1394, 2017 Cited by PubMed Abstract: Amino acid-dependent activation of the mechanistic target of rapamycin complex 1 (mTORC1) is mediated by Rag GTPases, which are recruited to the lysosome by the Ragulator complex consisting of p18, MP1, p14, HBXIP and C7orf59; however, the molecular mechanism is elusive. Here, we report the crystal structure of Ragulator, in which p18 wraps around the MP1-p14 and C7orf59-HBXIP heterodimers and the interactions of p18 with MP1, C7orf59, and HBXIP are essential for the assembly of Ragulator. There are two binding sites for the Roadblock domains of Rag GTPases: helix α1 of p18 and the two helices side of MP1-p14. The interaction of Ragulator with Rag GTPases is required for their cellular co-localization and can be competitively inhibited by C17orf59. Collectively, our data indicate that Ragulator functions as a scaffold to recruit Rag GTPases to lysosomal membrane in mTORC1 signaling. PubMed: 29123114DOI: 10.1038/s41467-017-01567-4 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.9 Å) |
構造検証レポート
検証レポート(詳細版)をダウンロード