Effluxed MoleculesEditThe 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.
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.
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. 
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.
- Yuzo: P-Glycoprotein: Introduction
- Yuzo: P-Glycoprotein: Biological function
- Yuzo: P-Glycoprotein: Biosynthesis
- Yuzo: P-Glycoprotein: Gene sequence
- Yuzo: P-Glycoprotein: Amino acid sequence and composition
- Yuzo: P-Glycoprotein: Domains and structural motifs
- Yuzo: P-Glycoprotein: Interactions with macromolecules and small molecules
- Yuzo: P-Glycoprotein: Molecular biodiversity and evolution
- Yuzo: P-Glycoprotein: Literature overview
- Yuzo: P-Glycoprotein: Online resources
- ↑ 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.
- ↑ Ford, J.M., and Hait, W.N. (1990). Pharmacology of drugs that alter multidrug resistance in cancer. Pharmacol Rev 42, 155–199.