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TitleCryo-EM Analysis of the Conformational Landscape of Human P-glycoprotein (ABCB1) During its Catalytic Cycle.
Journal, issue, pagesMol Pharmacol, Vol. 90, Issue 1, Page 35-41, Year 2016
Publish dateMay 11, 2016
AuthorsGabriel A Frank / Suneet Shukla / Prashant Rao / Mario J Borgnia / Alberto Bartesaghi / Alan Merk / Aerfa Mobin / Lothar Esser / Lesley A Earl / Michael M Gottesman / Di Xia / Suresh V Ambudkar / Sriram Subramaniam /
PubMed AbstractThe multidrug transporter P-glycoprotein (P-gp, ABCB1) is an ATP-dependent pump that mediates the efflux of structurally diverse drugs and xenobiotics across cell membranes, affecting drug ...The multidrug transporter P-glycoprotein (P-gp, ABCB1) is an ATP-dependent pump that mediates the efflux of structurally diverse drugs and xenobiotics across cell membranes, affecting drug pharmacokinetics and contributing to the development of multidrug resistance. Structural information about the conformational changes in human P-gp during the ATP hydrolysis cycle has not been directly demonstrated, although mechanistic information has been inferred from biochemical and biophysical studies conducted with P-gp and its orthologs, or from structures of other ATP-binding cassette transporters. Using single-particle cryo-electron microscopy, we report the surprising discovery that, in the absence of the transport substrate and nucleotides, human P-gp can exist in both open [nucleotide binding domains (NBDs) apart; inward-facing] and closed (NBDs close; outward-facing) conformations. We also probe conformational states of human P-gp during the catalytic cycle, and demonstrate that, following ATP hydrolysis, P-gp transitions through a complete closed conformation to a complete open conformation in the presence of ADP.
External linksMol Pharmacol / PubMed:27190212 / PubMed Central
MethodsEM (single particle)
Resolution12.0 - 22.0 Å
Structure data

EMDB-3421:
Electron cryo-microscopy of human P-glycoprotein: Apo state - closed conformation
Method: EM (single particle) / Resolution: 12.0 Å

EMDB-3422:
human P-Glycoprote in open conformation
Method: EM (single particle) / Resolution: 17.0 Å

EMDB-3423:
Electron cryo-microscopy of human P-glycoprotein: Apo state - closed conformation
Method: EM (single particle) / Resolution: 22.0 Å

EMDB-3424:
Electron cryo-microscopy of human P-glycoprotein: Apo state - open conformation
Method: EM (single particle) / Resolution: 22.0 Å

EMDB-3425:
Electron cryo-microscopy of human P-glycoprotein: ATP bound - closed conformation
Method: EM (single particle) / Resolution: 19.0 Å

EMDB-3426:
Electron cryo-microscopy of human P-glycoprotein: ATP bound state - open conformation
Method: EM (single particle) / Resolution: 21.0 Å

EMDB-3427:
Electron cryo-microscopy of human P-glycoprotein: Bound to ADP-Vi - closed conformation
Method: EM (single particle) / Resolution: 20.0 Å

EMDB-3428:
Electron cryo-microscopy of human P-glycoprotein: ADP bound state - open conformation #1
Method: EM (single particle) / Resolution: 21.0 Å

EMDB-3429:
Electron cryo-microscopy of human P-glycoprotein: ADP bound state - open conformation #2
Method: EM (single particle) / Resolution: 22.0 Å

EMDB-3430:
Electron cryo-microscopy of human P-glycoprotein: ADP bound state - open conformation #3
Method: EM (single particle) / Resolution: 22.0 Å

Source
  • Homo sapiens (human)
  • Mus musculus (house mouse)

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