Effluxed MoleculesEdit

The primary function of P-Glycoprotein is to efflux xenobiotics out of the cell's membrane. P-gp is most well known for effluxing many theraputic cancer molecules, effectively stopping treatment. P-gp primarily interacts with non polar molecules between 300-3000kDa in size. The hydrophobic pocket witin the membrane attracts foreign molecules and effluxes them using ATP.

A table on Selected Subtrates of P-gp (Ambudkar Et Al 1999)

ATP interactionEdit

P-gp can bind ATP at two locations. ATP is hydrolyzed and used to drive a conformational change. This change allows for P-gp to release the held molecule out of the cell. ATP is used once again to drive the shape back into the original form, resetting the process.[1]

MDR ModulatorsEdit

Modulators, are proteins that can regulate the function of transport proteins such as P-gp. certain modulators can increase the function of a transporter as well as repress it. Modulators are a relatively new discovery and are being used to help with cancer treatment. [2]

Currently, certain chemosensitizers are being used to inhibit P-gp function. These drugs help inhibit the protein allowing for the update of other theraputic drugs.

More InformationEdit

  1. Yuzo: P-Glycoprotein: Introduction
  2. Yuzo: P-Glycoprotein: Biological function
  3. Yuzo: P-Glycoprotein: Biosynthesis
  4. Yuzo: P-Glycoprotein: Gene sequence
  5. Yuzo: P-Glycoprotein: Amino acid sequence and composition
  6. Yuzo: P-Glycoprotein: Domains and structural motifs
  7. Yuzo: P-Glycoprotein: Interactions with macromolecules and small molecules
  8. Yuzo: P-Glycoprotein: Molecular biodiversity and evolution
  9. Yuzo: P-Glycoprotein: Literature overview
  10. Yuzo: P-Glycoprotein: Online resources


  1. Hrycyna, C.A., Ramachandra, M., Germann, U.A., Cheng, P.W., Pastan, I., and Gottesman, M.M. (1999). Both ATP sites of human P-glycoprotein are essential but not symmetric. Biochemistry 38, 13887–13899.
  2. Ford, J.M., and Hait, W.N. (1990). Pharmacology of drugs that alter multidrug resistance in cancer. Pharmacol Rev 42, 155–199.