The ATP‐bound inward‐open conformation of ABCC4 reveals asymmetric ATP binding for substrate transport

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作者信息关键词期刊信息基础信息归属信息摘要

成果类型：

期刊论文

作者：

Zhu, Yue;Xing, Xiaoke;Wang, Fuxing;Chen, Luojun;Zhong, Chunhui;...

通讯作者：

Han, SX;Zhang, PF;Liu, Z

作者机构：

[Han, Suxia; Zhu, Yue] Xi An Jiao Tong Univ, Affiliated Hosp 1, Dept Radiat Oncol, Xian 710061, Shaanxi, Peoples R China.

[Xing, Xiaoke; Chen, Luojun; Yao, Yi; Zhang, Pingfeng; Song, Qibin; Zhu, Yue] Wuhan Univ, Renmin Hosp, Canc Ctr, Wuhan 430060, Peoples R China.

[Zhong, Chunhui; Wang, Fuxing; Liu, Zheng] Chinese Univ Hong Kong, Sch Med, Kobilka Inst Innovat Drug Discovery, Shenzhen 518172, Guangdong, Peoples R China.

[Lu, Xiting; Yu, Zhanwang] Shenzhen Inst Techol, Sch Appl Biol, Shenzhen, Peoples R China.

[Yang, Yongbo] Cent China Normal Univ, Sch Life Sci, Wuhan, Peoples R China.

通讯机构：

[Han, SX ] X

[Zhang, PF ] W

[Liu, Z ] C

Xi An Jiao Tong Univ, Affiliated Hosp 1, Dept Radiat Oncol, Xian 710061, Shaanxi, Peoples R China.

Wuhan Univ, Renmin Hosp, Canc Ctr, Wuhan 430060, Peoples R China.

语种：

英文

关键词：

ABCC4;asymmetric ATP binding;degenerate NBD1;methotrexate;MRP4

期刊：

FEBS Letters

ISSN：

0014-5793

年：

2024

卷：

598

期：

页码：

1967-1980

DOI：

10.1002/1873-3468.14955

基金类别：

Renmin Hospital of Wuhan University; Kobilka Institute of Innovative Drug Discovery in the Chinese University of Hongkong (Shenzhen)

机构署名：

本校为其他机构

院系归属：

生命科学学院

摘要：

The multidrug resistance-associated protein (MRP) ABCC4 facilitates substrate transport across the cytoplasmic membrane, crucial for normal physiology and mediating multidrug resistance in tumor cells. Despite intensive studies on MRPs, ABCC4's transport mechanism remains incompletely understood. In this study, we unveiled an inward-open conformation with an ATP bound to degenerate NBD1. Additionally, we captured the structure with both ATP and substrate co-bound in the inward-open state. Our findings uncover the asymmetric ATP binding in ABCC4 and provide insights into substrate binding and t...

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The ATP‐bound inward‐open conformation of ABCC4 reveals asymmetric ATP binding for substrate transport

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