7DKL
Crystal structure of the tandem DEP domains of DEPTOR
Summary for 7DKL
| Entry DOI | 10.2210/pdb7dkl/pdb |
| Descriptor | DEP domain-containing mTOR-interacting protein (2 entities in total) |
| Functional Keywords | mtor inhibitor, pa binding protein, dep domain, anionic lipid binding protein, lipid binding protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 26058.98 |
| Authors | Weng, Z.F.,Shen, X.X.,Liu, Y.F. (deposition date: 2020-11-24, release date: 2021-12-08, Last modification date: 2023-11-29) |
| Primary citation | Weng, Z.,Shen, X.,Zheng, J.,Liang, H.,Liu, Y. Structural Basis of DEPTOR to Recognize Phosphatidic Acid Using its Tandem DEP Domains. J.Mol.Biol., 433:166989-166989, 2021 Cited by PubMed Abstract: DEP domain containing mTOR-interacting protein (DEPTOR) plays pivotal roles in regulating metabolism, growth, autophagy and apoptosis by functions as an endogenous inhibitor of mTOR signaling pathway. Activated by phosphatidic acid, a second messenger in mTOR signaling, DEPTOR dissociates from mTORC1 complex with unknown mechanism. Here, we present a 1.5 Å resolution crystal structure, which shows that the N-terminal two tandem DEP domains of hDEPTOR fold into a dumbbell-shaped structure, protruding the characteristic β-hairpin arms of DEP domains on each side. An 18 amino acids DDEX motif at the end of DEP2 interacts with DEP1 and stabilizes the structure. Biochemical studies showed that the tandem DEP domains directly interact with phosphatidic acid using two distinct positively charged patches. These results provide insights into mTOR activation upon phosphatidic acid stimulation. PubMed: 33865870DOI: 10.1016/j.jmb.2021.166989 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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