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A new structural model for P-glycoprotein

P M Jones1, A M George

  • 1Department of Cell and Molecular Biology, University of Technology Sydney, Sydney, NSW 2007, Australia.

The Journal of Membrane Biology
|December 5, 1998
PubMed
Summary
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Multidrug resistance in cancer is a major problem. This study proposes a new structural model for P-glycoprotein, an ABC transporter, revealing drug binding and translocation sites.

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Pharmacology

Background:

  • Multidrug resistance (MDR) to anti-cancer drugs is a significant clinical challenge.
  • P-glycoprotein, encoded by the human MDR1 gene, is a key ABC transporter protein responsible for MDR.
  • Existing structural models for P-glycoprotein are incomplete despite extensive mutagenesis and labeling studies.

Purpose of the Study:

  • To propose a novel, comprehensive structural model for human P-glycoprotein.
  • To elucidate the structural basis of drug binding and translocation mediated by P-glycoprotein.
  • To reconcile previous experimental data with a new structural framework.

Main Methods:

  • Development of a new structural model for P-glycoprotein based on existing data.

Related Experiment Videos

  • Analysis of amino acid sequence alignments of P-glycoprotein isoforms.
  • Delineation of potential drug binding and translocation sites within the proposed model.

    • Main Results:

    • A new model for P-glycoprotein is proposed, featuring membrane-embedded beta-barrels and underlying helix bundles.
    • Each ATP binding domain contributes specific beta-strands and an alpha-helix to the overall structure.
    • The proposed model successfully integrates and explains diverse experimental findings, including mutational, kinetic, and labeling data.

    Conclusions:

    • The novel structural model provides a framework for understanding P-glycoprotein function in multidrug resistance.
    • The identified drug binding and translocation sites are consistent with experimental evidence.
    • This model advances our understanding of ABC transporter mechanisms and offers potential targets for overcoming drug resistance.