7DKL

Crystal structure of the tandem DEP domains of DEPTOR

7DKL の概要

• エントリーDOI: 10.2210/pdb7dkl/pdb
• 分子名称: DEP domain-containing mTOR-interacting protein (2 entities in total)
• 機能のキーワード: mtor inhibitor, pa binding protein, dep domain, anionic lipid binding protein, lipid binding protein
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 26058.98

構造登録者

Weng, Z.F.,Shen, X.X.,Liu, Y.F. (登録日: 2020-11-24, 公開日: 2021-12-08, 最終更新日: 2023-11-29)

主引用文献

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

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: 33865870
DOI: 10.1016/j.jmb.2021.166989

実験手法

X-RAY DIFFRACTION (1.5 Å)