5ef5 | pdb_00005ef5

Crystal structure of Chaetomium thermophilum Raptor

spinqualitylabelsall models 5ef5, resolution 4.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5ef5 is a 2 chain structure with sequence from Chaetomium thermophilum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 4.3Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Target of rapamycin (TOR), a conserved protein kinase and central controller of cell growth, functions in two structurally and functionally distinct complexes: TORC1 and TORC2. Dysregulation of mammalian TOR (mTOR) signaling is implicated in pathologies that include diabetes, cancer, and neurodegeneration. We resolved the architecture of human mTORC1 (mTOR with subunits Raptor and mLST8) bound to FK506 binding protein (FKBP)-rapamycin, by combining cryo-electron microscopy at 5.9 angstrom resolution with crystallographic studies of Chaetomium thermophilum Raptor at 4.3 angstrom resolution. The structure explains how FKBP-rapamycin and architectural elements of mTORC1 limit access to the recessed active site. Consistent with a role in substrate recognition and delivery, the conserved amino-terminal domain of Raptor is juxtaposed to the kinase active site. Architecture of human mTOR complex 1.,Aylett CH, Sauer E, Imseng S, Boehringer D, Hall MN, Ban N, Maier T Science. 2016 Jan 1;351(6268):48-52. doi: 10.1126/science.aaa3870. Epub 2015 Dec , 17. PMID:26678875 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Raptor

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