6EHR

The crystal structure of the human LAMTOR-RagA CTD-RagC CTD complex

6EHR の概要

• エントリーDOI: 10.2210/pdb6ehr/pdb
• 関連するPDBエントリー: 6EHP
• 分子名称: Ragulator complex protein LAMTOR3, Ragulator complex protein LAMTOR2, Ragulator complex protein LAMTOR5, ... (7 entities in total)
• 機能のキーワード: scaffolding complex, rag-gtpases, mtor, ragulator, mtorc1, signaling protein
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 97142.93

構造登録者

Scheffzek, K.,Naschberger, A. (登録日: 2017-09-14, 公開日: 2017-10-04, 最終更新日: 2024-05-08)

主引用文献

de Araujo, M.E.G.,Naschberger, A.,Furnrohr, B.G.,Stasyk, T.,Dunzendorfer-Matt, T.,Lechner, S.,Welti, S.,Kremser, L.,Shivalingaiah, G.,Offterdinger, M.,Lindner, H.H.,Huber, L.A.,Scheffzek, K.
Crystal structure of the human lysosomal mTORC1 scaffold complex and its impact on signaling.
Science, 358:377-381, 2017

PubMed Abstract: The LAMTOR [late endosomal and lysosomal adaptor and MAPK (mitogen-activated protein kinase) and mTOR (mechanistic target of rapamycin) activator] complex, also known as "Ragulator," controls the activity of mTOR complex 1 (mTORC1) on the lysosome. The crystal structure of LAMTOR consists of two roadblock/LC7 domain-folded heterodimers wrapped and apparently held together by LAMTOR1, which assembles the complex on lysosomes. In addition, the Rag guanosine triphosphatases (GTPases) associated with the pentamer through their carboxyl-terminal domains, predefining the orientation for interaction with mTORC1. In vitro reconstitution and experiments with site-directed mutagenesis defined the physiological importance of LAMTOR1 in assembling the remaining components to ensure fidelity of mTORC1 signaling. Functional data validated the effect of two short LAMTOR1 amino acid regions in recruitment and stabilization of the Rag GTPases.

PubMed: 28935770
DOI: 10.1126/science.aao1583

実験手法

X-RAY DIFFRACTION (2.898 Å)