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Molecular DiversityEdit

P-Glycoprotein is found in a variety of different species. Due to the direct link with cancer research, human and mouse P-gp are studied.

P-gp has a number of polymorphisms, most of which seem to be in the transmembrane region. It has been suggested that these polymorphisms can cause changes in substrate binding affinity.

Diversity within ABC transportersEdit

P-gp is a transporter within the ABC family. Specifically P-gp is also known as ABCB1. Many other ABC transporters have similar structure to P-gp, but can transport different types of molecules. [1] These polymorphisms could have serious impacts on health of a cell. ABC transporters in the A, B, C and G family have all been shown to confer drug resistance. A similar protein MRP1 (ABC C1) has a very similar structure to P-gp, but instead effluxes anionic compunds. MRP1 and P-gp even have varying rates of expression.

Evolution of P-GlycoproteinEdit

It is hypothesized that ABC transporters in general arose from a duplication of the ABC subunits. The ability for P-gp to efflux xenobiotics has a huge impact on cell survivability.[2] This can explain the fact that P-gp is highly conserved.

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

ReferencesEdit

  1. Fung, K.L., and Gottesman, M.M. (2009). A synonymous polymorphism in a common MDR1 (ABCB1) haplotype shapes protein function. Biochim Biophys Acta 1794, 860–871.
  2. Moitra, K., and Dean, M. (2011). Evolution of ABC transporters by gene duplication and their role in human disease. Biol. Chem. 392, 29–37.

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