南华大学心血管疾病研究所,南华大学心血管疾病研究所,南华大学心血管疾病研究所,南华大学心血管疾病研究所,医学研究实验中心
国家自然科学基金资助项目(81570408)
Institute of Cardiovascular Research, University of South China, Hengyang 421001, Hunan, China,Institute of Cardiovascular Research, University of South China, Hengyang 421001, Hunan, China,Institute of Cardiovascular Research, University of South China, Hengyang 421001, Hunan, China,Institute of Cardiovascular Research, Medical Research Experiment Center, University of South China, Hengyang 421001, Hunan, China
This work was supported by a grant from The National Natural Science Foundation of China (81570408)
三磷酸腺苷结合盒转运体A1(ATP-binding cassette transporter A1,ABCA1) 是一种具有调节细胞内胆固醇流出等功能的跨膜蛋白,与动脉粥样硬化(Atherosclerosis,AS)发生发展密切相关,但其结构基础和分子机制仍不明确.近日,清华大学结构生物学高精尖创新中心的研究团队(Cell,2017,169:1228-1239)利用冷冻电子显微镜技术,首次获得了重组人ABCA1在未结合ATP状态下近原子级分辨率的结构,并提出了ABCA1通过“lateral access”方式转运细胞内胆固醇的学说.
ATP binding cassette transporter A1 (ABCA1) is a transmembrane protein that regulates intracellular cholesterol efflux and is closely related to the development of atherosclerosis (AS). But its structure and molecular mechanisms are still unclear. Recently an issue published on Cell (2017,169:1228-1239) by researchers from Beijing Advanced Innovation Center for Structural Biology, Tsinghua University, China reported the cryo-EM structure of human ABCA1 and suggested a plausible ‘‘lateral access’’ mechanisms for ABCA1-mediated lipid export.
王斯琦,张敏,陈凌燕,唐朝克. ABCA1结构对胆固醇流出的影响[J].生物化学与生物物理进展,2017,44(9):806-808
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