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The first structure of human Golm1 coiled coil domain reveals an unexpected tetramer and highlights its structural diversity

文献类型：期刊论文

作者Bai, Wenfeng3,5; Li, Bowen4; Wu, Pei4; Li, Xinzhu1,5; Huang, Xiaochen4; Shi, Ning3,4; Yang, Congcong3; Hu, Fen2; Xie, Xi4,5
刊名INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
出版日期2024-08-01
卷号275页码:14
关键词Golm1 Serum Golm1 Coiled coil domain Tetramer Crystal structure
ISSN号0141-8130
DOI10.1016/j.ijbiomac.2024.133624
通讯作者Yang, Congcong(982747682@qq.com) ; Hu, Fen(fenhu@fjmu.edu.cn) ; Xie, Xi(xiexi@simm.ac.cn)
英文摘要Golgi membrane protein 1 (Golm1), a transmembrane protein with diverse subcellular localizations, has garnered significant attention in recent years due to its strong association with the development and progression of liver diseases and numerous cancers. Interestingly, although Golm1 is a membrane protein, the C-terminal of Golm1, which contains a coiled coil domain and a flexible acid region, can also be detected in the plasma of patients with various liver diseases. Notably, the coiled coil domain of serum Golm1 is postulated to play a pivotal role in physiological and pathological functions. However, little is currently known about the structure of this coiled coil domain and the full-length protein, which may limit our understanding of Golm1. Therefore, this study aims to address this gap in knowledge and reports the first crystal structure of the coiled coil domain of Golm1 at a resolution of 2.28 & Aring;. Meanwhile, we have also confirmed that the Golm1 coiled coil domain in solution can form tetramer. Our results reveal that Golm1 can form a novel tetrameric structure that differs from the previous reported dimeric structure Golm1 could assemble, which may provide novel insights into the diversity of physiological functions and pathological roles.
WOS关键词PHOSPHOPROTEIN 2 GOLPH2 ; GOLGI PROTEIN 73 ; MAMMALIAN-CELLS ; WATER-MOLECULES ; EXPRESSION ; GP73 ; DIFFRACTION ; PROGRESSION ; ARCIMBOLDO ; MEDIATE
WOS研究方向Biochemistry & Molecular Biology ; Chemistry ; Polymer Science
语种英语
WOS记录号WOS:001266500600001
出版者ELSEVIER
源URL[http://119.78.100.183/handle/2S10ELR8/312267]  
专题新药研究国家重点实验室
通讯作者Yang, Congcong; Hu, Fen; Xie, Xi
作者单位1.Nanjing Univ Chinese Med, Sch Chinese Mat Med, Nanjing 210023, Peoples R China
2.Fujian Med Univ, Sch Basic Med Sci, Dept Etiol, Key Lab Gastrointestinal Canc,Minist Educ, Fuzhou, Peoples R China
3.Shanghai Univ Tradit Chinese Med, Shanghai TCM Integrated Hosp, Shanghai 200082, Peoples R China
4.Chinese Acad Sci, Fujian Inst Res Struct Matter, State Key Lab Struct Chem, Fuzhou 350002, Peoples R China
5.Chinese Acad Sci, Shanghai Inst Mat Med, State Key Lab Drug Res, Shanghai 201203, Peoples R China
推荐引用方式
GB/T 7714		 Bai, Wenfeng,Li, Bowen,Wu, Pei,et al. The first structure of human Golm1 coiled coil domain reveals an unexpected tetramer and highlights its structural diversity[J]. INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES,2024,275:14.
APA Bai, Wenfeng.,Li, Bowen.,Wu, Pei.,Li, Xinzhu.,Huang, Xiaochen.,...&Xie, Xi.(2024).The first structure of human Golm1 coiled coil domain reveals an unexpected tetramer and highlights its structural diversity.INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES,275,14.
MLA Bai, Wenfeng,et al."The first structure of human Golm1 coiled coil domain reveals an unexpected tetramer and highlights its structural diversity".INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES 275(2024):14.

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来源：上海药物研究所

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