Cryo-EM structures reveal the dynamic transformation of human alpha-2-macroglobulin working as a protease inhibitor

被引：0

作者：

Xiaoxing Huang ^{[1
]}

Youwang Wang ^{[1
,2
]}

Cong Yu ^{[1
,2
]}

Hui Zhang ^{[1
,2
]}

Qiang Ru ^{[3
]}

Xinxin Li ^{[1
,2
]}

Kai Song ^{[1
]}

Min Zhou ^{[1
]}

Ping Zhu ^{[1
,2
]}

机构：

[1] National Laboratory of Biomacromolecules,CAS Center for Excellence in Biomacromolecules,Institute of Biophysics,Chinese Academy of Sciences

[2] University of Chinese Academy of Sciences

[3] The Institute of Medicinal Plant Development,Chinese Academy of Medical Sciences (CAMS) and Peking Union Medical College (PUMC)

来源：

Science China(Life Sciences) | 2022年 / 12期

基金：

中国国家自然科学基金;

关键词：

D O I：

暂无

中图分类号：

R341 [];

学科分类号：

1001 ;

摘要：

Human alpha-2-macroglobulin is a well-known inhibitor of a broad spectrum of proteases and plays important roles in immunity,inflammation,and infections.Here,we report the cryo-EM structures of human alpha-2-macroglobulin in its native state,induced state transformed by its authentic substrate,human trypsin,and serial intermediate states between the native and fully induced states.These structures exhibit distinct conformations,which reveal the dynamic transformation of alpha-2-macroglobulin that acts as a protease inhibitor.The results shed light on the molecular mechanism of alpha-2-macroglobulin in entrapping substrates.

引用

页码：2491 / 2504

页数：14

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