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Structure paper

TitleStructure of the human multidrug transporter ABCG2.
Journal, issue, pagesNature, Vol. 546, Issue 7659, Page 504-509, Year 2017
Publish dateJun 22, 2017
AuthorsNicholas M I Taylor / Ioannis Manolaridis / Scott M Jackson / Julia Kowal / Henning Stahlberg / Kaspar P Locher /
PubMed AbstractABCG2 is a constitutively expressed ATP-binding cassette (ABC) transporter that protects many tissues against xenobiotic molecules. Its activity affects the pharmacokinetics of commonly used drugs ...ABCG2 is a constitutively expressed ATP-binding cassette (ABC) transporter that protects many tissues against xenobiotic molecules. Its activity affects the pharmacokinetics of commonly used drugs and limits the delivery of therapeutics into tumour cells, thus contributing to multidrug resistance. Here we present the structure of human ABCG2 determined by cryo-electron microscopy, providing the first high-resolution insight into a human multidrug transporter. We visualize ABCG2 in complex with two antigen-binding fragments of the human-specific, inhibitory antibody 5D3 that recognizes extracellular loops of the transporter. We observe two cholesterol molecules bound in the multidrug-binding pocket that is located in a central, hydrophobic, inward-facing translocation pathway between the transmembrane domains. Combined with functional in vitro analyses, our results suggest a multidrug recognition and transport mechanism of ABCG2, rationalize disease-causing single nucleotide polymorphisms and the allosteric inhibition by the 5D3 antibody, and provide the structural basis of cholesterol recognition by other G-subfamily ABC transporters.
External linksNature / PubMed:28554189
MethodsEM (single particle) / X-ray diffraction
Resolution1.498 - 3.78 Å
Structure data

3654

5nj3

5njg

EMDB-3654: Structure of an ABC transporter
PDB-5nj3: Structure of an ABC transporter: complete structure
PDB-5njg: Structure of an ABC transporter: part of the structure that could be built de novo
Method: EM (single particle) / Resolution: 3.78 Å

PDB-5niv:
Crystal structure of 5D3 Fab
Method: X-RAY DIFFRACTION / Resolution: 1.498 Å

Chemicals

ChemComp-HOH:
WATER / Water

Source
  • homo sapiens (human)
  • mus musculus (house mouse)
KeywordsIMMUNE SYSTEM / Fab / ABCG2 / inhibitor / TRANSPORT PROTEIN / ABC transporter

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