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-Structure paper
| タイトル | Cryo-EM reveals cholesterol binding in the lysosomal GPCR-like protein LYCHOS. |
|---|---|
| ジャーナル・号・ページ | Nat Struct Mol Biol, Vol. 32, Issue 5, Page 896-904, Year 2025 |
| 掲載日 | 2025年1月17日 |
著者 | Jie Zhao / Qingya Shen / Xihao Yong / Xin Li / Xiaowen Tian / Suyue Sun / Zheng Xu / Xiaoyu Zhang / Lu Zhang / Hao Yang / Zhenhua Shao / Haoxing Xu / Yiyang Jiang / Yan Zhang / Wei Yan / ![]() |
| PubMed 要旨 | Cholesterol plays a pivotal role in modulating the activity of mechanistic target of rapamycin complex 1 (mTOR1), thereby regulating cell growth and metabolic homeostasis. LYCHOS, a lysosome- ...Cholesterol plays a pivotal role in modulating the activity of mechanistic target of rapamycin complex 1 (mTOR1), thereby regulating cell growth and metabolic homeostasis. LYCHOS, a lysosome-localized G-protein-coupled receptor-like protein, emerges as a cholesterol sensor and is capable of transducing the cholesterol signal to affect the mTORC1 function. However, the precise mechanism by which LYCHOS recognizes cholesterol remains unknown. Here, using cryo-electron microscopy, we determined the three-dimensional structural architecture of LYCHOS in complex with cholesterol molecules, revealing a unique arrangement of two sequential structural domains. Through a comprehensive analysis of this structure, we elucidated the specific structural features of these two domains and their collaborative role in the process of cholesterol recognition by LYCHOS. |
リンク | Nat Struct Mol Biol / PubMed:39824976 |
| 手法 | EM (単粒子) |
| 解像度 | 2.83 Å |
| 構造データ | EMDB-38930, PDB-8y56: |
| 化合物 | ![]() ChemComp-NA: ![]() ChemComp-CLR: ![]() ChemComp-DKB: ![]() ChemComp-HOH: |
| 由来 |
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キーワード | MEMBRANE PROTEIN / cholesterol / lysosome |
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