| First Author | Gros P | Year | 1986 |
| Journal | Cell | Volume | 47 |
| Issue | 3 | Pages | 371-80 |
| PubMed ID | 3768958 | Mgi Jnum | J:8447 |
| Mgi Id | MGI:56913 | Doi | 10.1016/0092-8674(86)90594-5 |
| Citation | Gros P, et al. (1986) Mammalian multidrug resistance gene: complete cDNA sequence indicates strong homology to bacterial transport proteins. Cell 47(3):371-80 |
| abstractText | 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. |
