Abstract:
:Multidrug transporters are involved in mediating the failure of chemotherapy in treating several serious diseases. The archetypal multidrug transporter P-glycoprotein (P-gp) confers resistance to a large number of chemically and functionally unrelated anti-cancer drugs by mediating efflux from cancer cells. The ability to efflux such a large number of drugs remains a biological enigma and the lack of mechanistic understanding of the translocation pathway used by P-gp prevents rational design of compounds to inhibit its function. The translocation pathway is critically dependent on ATP hydrolysis and drug interaction with P-gp is possible at one of a multitude of allosterically linked binding sites. However, aspects such as coupling stoichiometry, molecular properties of binding sites and the nature of conformational changes remain unresolved or the centre of considerable controversy. The present review attempts to utilise the available data to generate a detailed sequence of events in the translocation pathway for this dexterous protein.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Callaghan R,Ford RC,Kerr IDdoi
10.1016/j.febslet.2005.11.083keywords:
subject
Has Abstractpub_date
2006-02-13 00:00:00pages
1056-63issue
4eissn
0014-5793issn
1873-3468pii
S0014-5793(05)01476-6journal_volume
580pub_type
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