P-glycoprotein structure and evolutionary homologies

Irene Bosch, James M. Croop

Research output: Contribution to journalArticle

13 Scopus citations

Abstract

Analysis of multidrug resistant cell lines has led to the identification of the P-glycoprotein multigene family. Two of the three classes of mammalian P-glycoproteins have the ability to confer cellular resistance to a broad range of structurally and functionally diverse cytotoxic agents. P-glycoproteins are integral membrane glycoproteins comprised of two similar halves, each consisting of six membrane spanning domains followed by a cytoplasmic domain which includes a nucleotide binding fold. The P-glycoprotein is a member of a large superfamily of transport proteins which utilize ATP to translocate a wide range of substrates across biological membranes. This superfamily includes transport complexes comprised of multicomponent systems, half P-glycoproteins and P-glycoprotein-like homologs which appear to require approximately 12 α-helical transmembrane domains and two nucleotide binding folds for substrate transport. P-glycoprotein homologs have been isolated and characterized from a wide range of species. Amino acid sequences, the similarities between the halves and intron/exon boundaries have been compared to understand the evolutionary origins of the P-glycoprotein.

Original languageEnglish (US)
Pages (from-to)1-30
Number of pages30
JournalCytotechnology
Volume27
Issue number1-3
StatePublished - Dec 1 1998

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Keywords

  • ABC transporters
  • MDR
  • Multidrug resistance
  • P-glycoprotein

ASJC Scopus subject areas

  • Cell Biology
  • Biotechnology
  • Clinical Biochemistry

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