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Self-Assembly of Gamma-Modified Peptide Nucleic Acids into Complex Nanostructures in Organic Solvent Mixtures
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Nucleotide-induced structural changes in P-glycoprotein observed by electron microscopy.

Jyh-Yeuan Lee1, Ina L Urbatsch, Alan E Senior

  • 1Department of Biochemistry, University of California, Riverside, California 92521, USA.

The Journal of Biological Chemistry
|December 21, 2007
PubMed
Summary
This summary is machine-generated.

Human P-glycoprotein (Pgp), a multidrug efflux pump, shares a similar structure with mouse Pgp. Nucleotide binding induces conformational changes, suggesting Pgp functions by switching between states.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Medicine

Background:

  • P-glycoprotein (Pgp) is an ATP-driven multidrug efflux pump.
  • Overexpression of Pgp in cancer can cause chemotherapy failure.

Purpose of the Study:

  • To analyze the structure of human Pgp using electron microscopy.
  • To investigate the conformational changes of Pgp in response to nucleotide binding.

Main Methods:

  • Two-dimensional crystallization of cysteine-free human Pgp using lipid monolayer technique.
  • Electron microscopy of crystallized Pgp in the absence and presence of nucleotides.
  • Calculation of a low-resolution 3D model using tilted specimens.

Main Results:

  • Human Pgp exhibits a structure similar to mouse Pgp.
  • Pgp exists in at least two major nucleotide-dependent conformations: one with an open central cavity and one with a closed cavity.
  • Intermediate conformations were observed with specific nucleotide/vanadate combinations.

Conclusions:

  • Pgp functions by nucleotide-dependent conformational switching between major states.
  • This structural insight contributes to understanding multidrug ABC transporter mechanisms.