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Structure paper

TitleStructures of human bile acid exporter ABCB11 reveal a transport mechanism facilitated by two tandem substrate-binding pockets.
Journal, issue, pagesCell Res, Vol. 32, Issue 5, Page 501-504, Year 2022
Publish dateJan 18, 2022
AuthorsLiang Wang / Wen-Tao Hou / Jie Wang / Da Xu / Cong Guo / Linfeng Sun / Ke Ruan / Cong-Zhao Zhou / Yuxing Chen /
External linksCell Res / PubMed:35043010 / PubMed Central
MethodsEM (single particle)
Resolution3.6 - 3.7 Å
Structure data

30870

7dv5

EMDB-30870, PDB-7dv5:
Human bile salt exporter ABCB11 in complex with taurocholate
Method: EM (single particle) / Resolution: 3.7 Å

30938

7e1a

EMDB-30938, PDB-7e1a:
Human bile salt exporter ABCB11 in complex with taurocholate
Method: EM (single particle) / Resolution: 3.66 Å

EMDB-32261: huamn bile salt exporter ABCB11 with N-terminal truncated
Method: EM (single particle) / Resolution: 3.6 Å

Chemicals

ChemComp-TCH:
TAUROCHOLIC ACID

Source
  • homo sapiens (human)
KeywordsTRANSLOCASE / ABC transporter / liver / MEMBRANE PROTEIN

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