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6EHR

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

Summary for 6EHR
Entry DOI10.2210/pdb6ehr/pdb
Related6EHP
DescriptorRagulator complex protein LAMTOR3, Ragulator complex protein LAMTOR2, Ragulator complex protein LAMTOR5, ... (7 entities in total)
Functional Keywordsscaffolding complex, rag-gtpases, mtor, ragulator, mtorc1, signaling protein
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains7
Total formula weight97142.93
Authors
Scheffzek, K.,Naschberger, A. (deposition date: 2017-09-14, release date: 2017-10-04, Last modification date: 2024-05-08)
Primary citationde 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.898 Å)
Structure validation

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数据于2024-11-06公开中

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