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TitleMolecular structure of human P-glycoprotein in the ATP-bound, outward-facing conformation.
Journal, issue, pagesScience, Vol. 359, Issue 6378, Page 915-919, Year 2018
Publish dateFeb 23, 2018
AuthorsYoungjin Kim / Jue Chen /
PubMed AbstractThe multidrug transporter permeability (P)-glycoprotein is an adenosine triphosphate (ATP)-binding cassette exporter responsible for clinical resistance to chemotherapy. P-glycoprotein extrudes toxic ...The multidrug transporter permeability (P)-glycoprotein is an adenosine triphosphate (ATP)-binding cassette exporter responsible for clinical resistance to chemotherapy. P-glycoprotein extrudes toxic molecules and drugs from cells through ATP-powered conformational changes. Despite decades of effort, only the structures of the inward-facing conformation of P-glycoprotein are available. Here we present the structure of human P-glycoprotein in the outward-facing conformation, determined by cryo-electron microscopy at 3.4-angstrom resolution. The two nucleotide-binding domains form a closed dimer occluding two ATP molecules. The drug-binding cavity observed in the inward-facing structures is reorientated toward the extracellular space and compressed to preclude substrate binding. This observation indicates that ATP binding, not hydrolysis, promotes substrate release. The structure evokes a model in which the dynamic nature of P-glycoprotein enables translocation of a large variety of substrates.
External linksScience / PubMed:29371429
MethodsEM (single particle)
Resolution3.4 Å
Structure data

7325

6c0v

EMDB-7325, PDB-6c0v:
Molecular structure of human P-glycoprotein in the ATP-bound, outward-facing conformation
Method: EM (single particle) / Resolution: 3.4 Å

Chemicals

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM / Adenosine triphosphate

ChemComp-MG:
Unknown entry

Source
  • homo sapiens (human)
KeywordsTRANSPORT PROTEIN / ABC transporter; ABCB1; P-glycoprotein; cryo-EM; multidrug resistance / Structural Genomics / PSI-2 / Protein Structure Initiative

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