Ragulator complex: Difference between revisions
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<StructureSection load='5y39' size='340' side='right' caption='Human ragulator complex proteins: LAMTOR1 coiled coil domain (grey) + LAMTOR2 roadblock domain (green) + LAMTOR3 roadblock domain (pink) + LAMTOR4 roadblock domain (yellow) + LAMTOR5 roadblock domain (magenta) PDB code [[5y39]]' scene=''> | <StructureSection load='5y39' size='340' side='right' caption='Human ragulator complex proteins: LAMTOR1 coiled coil domain (grey and cyan) + LAMTOR2 roadblock domain (green and red) + LAMTOR3 roadblock domain (pink and gold) + LAMTOR4 roadblock domain (yellow and wheat) + LAMTOR5 roadblock domain (magenta and blue) PDB code [[5y39]]' scene=''> | ||
The '''ragulator complex''' (Lamtor) is a pentamer which recruits mTORC1 in the rapamycin (mTOR) signal-transduction pathway and activates it<ref>PMID:29285400</ref>. | The '''ragulator complex''' (Lamtor) is a pentamer which recruits mTORC1 in the rapamycin (mTOR) signal-transduction pathway and activates it<ref>PMID:29285400</ref>. | ||
Revision as of 11:32, 25 October 2018
The ragulator complex (Lamtor) is a pentamer which recruits mTORC1 in the rapamycin (mTOR) signal-transduction pathway and activates it[1]. FunctionDiseaseRelevanceStructural highlights |
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3D structures of ragulator complex3D structures of ragulator complex
Updated on 25-October-2018
6b9x - hLAMTOR1 + LAMTOR2 + LAMTOR3 + LAMTOR4 + hepatitis B virus interacting protein - human
5y39, 5y3a, 6ehp - hLAMTOR1 + LAMTOR2 + LAMTOR3 + LAMTOR4 + LAMTOR5
5x6u - hLAMTOR1 (mutant) + LAMTOR2 + LAMTOR3 + LAMTOR4 + LAMTOR5
6ehr - hLAMTOR1 + LAMTOR2 + LAMTOR3 + LAMTOR4 + LAMTOR5 + Ras-related GTP-binding proteins A, C
5x6v - hLAMTOR1 (mutant) + LAMTOR2 + LAMTOR3 + LAMTOR4 + LAMTOR5 + Ras-related GTP-binding proteins A, C
5vok, 5y38 - hLAMTOR4 + LAMTOR5
ReferencesReferences
- ↑ Mu Z, Wang L, Deng W, Wang J, Wu G. Structural insight into the Ragulator complex which anchors mTORC1 to the lysosomal membrane. Cell Discov. 2017 Dec 26;3:17049. doi: 10.1038/celldisc.2017.49. eCollection, 2017. PMID:29285400 doi:http://dx.doi.org/10.1038/celldisc.2017.49