Volume 30, No 7, Jul 2020

ISSN: 1001-0602 
EISSN: 1748-7838 2018 
impact factor 17.848* 
(Clarivate Analytics, 2019)

Volume 30 Issue 7, July 2020: 623-625

LETTERS TO THE EDITOR

Cryo-EM structure of human bile salts exporter ABCB11

Liang Wang¹ , Wen-Tao Hou¹ , Li Chen¹ , Yong-Liang Jiang¹ , Da Xu¹ , Linfeng Sun^1,2,* , Cong-Zhao Zhou^1,* , Yuxing Chen^1,*

¹Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui, China
²CAS Centre for Excellence in Molecular Cell Science, University of Science and Technology of China, 230027 Hefei, Anhui, China
These authors contributed equally: Liang Wang, Wen-Tao Hou Correspondence: Linfeng Sun(sunlf17@ustc.edu.cn)Cong-Zhao Zhou(zcz@ustc.edu.cn)Yuxing Chen(cyxing@ustc.edu.cn)

Dear Editor,

Bile is a complex aqueous secretion produced by the liver that facilitates the digestion of lipids in the small intestine. A group of ATP binding cassette (ABC) transporters localizing at the apical canalicular domain of hepatocytes are responsible for the secretion of the bile organic solutes to the bile canaliculi,1 including organic anions, cholesterol, bile salts, glutathione, organic cations and phospholipid (Fig. 1a). To date, the 3-D structures of ABCG2, ABCG5/G8, ABCB1, ABCB4 have been reported,2,3 leaving the structures of ABCB11 and ABCC2 unknown, despite we can get some information from the homologous structures of ABCC1,4 ABCB1 and ABCB4.

https://doi.org/10.1038/s41422-020-0302-0

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