Mammalian multidrug resistance gene

Complete cDNA sequence indicates strong homology to bacterial transport proteins

Philippe Gros, James Croop, David Housman

Research output: Contribution to journalArticle

828 Citations (Scopus)

Abstract

The complete nucleotide and primary structure (1276 amino acids) of a full length mdr cDNA capable of conferring a complete multidrug-resistant phenotype is presented. The deduced amino acid sequence suggests that mdr is a membrane glycoprotein which includes six pairs of transmembrane domains and a cluster of potentially N-linked glycosylation sites near the amino terminus. A striking feature of the protein is an internal duplication that includes approximately 500 amino acids. Each duplicated segment includes a consensus ATP-binding site. Amino acid homology is observed between the mdr gene and a series of bacterial transport genes. This strong homology suggests that a highly conserved functional unit involved in membrane transport is present in the mdr polypeptide. We propose that an energy-dependent transport mechanism is responsible for the multidrug-resistant phenotype.

Original languageEnglish (US)
Pages (from-to)371-380
Number of pages10
JournalCell
Volume47
Issue number3
DOIs
StatePublished - Nov 7 1986
Externally publishedYes

Fingerprint

MDR Genes
Bacterial Proteins
Carrier Proteins
Complementary DNA
Genes
Amino Acids
Phenotype
Bacterial Genes
Membrane Glycoproteins
Glycosylation
Amino Acid Sequence
Nucleotides
Adenosine Triphosphate
Binding Sites
Peptides
Membranes
Proteins

ASJC Scopus subject areas

  • Cell Biology
  • Molecular Biology
  • Medicine(all)

Cite this

Mammalian multidrug resistance gene : Complete cDNA sequence indicates strong homology to bacterial transport proteins. / Gros, Philippe; Croop, James; Housman, David.

In: Cell, Vol. 47, No. 3, 07.11.1986, p. 371-380.

Research output: Contribution to journalArticle

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