Purification and structural analyses of ABCG2

Christopher A. McDevitt, Richard Collins, Ian D. Kerr, Richard Callaghan*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

27 Citations (Scopus)


ABCG2 is best known as a multidrug transporter capable of conferring resistance to cancer cells. However, the protein is also inherently expressed in numerous barrier tissues and intriguingly within hematopoietic stem cells. Unlike its partners ABCB1 and ABCC1, there is considerably less information available on the molecular mechanism of ABCG2. The transporter has a distinct topology and is presumed to function as a homodimer. However, a number of biochemical studies have presented data to suggest that the protein adopts higher order oligomers. This review focuses on this controversial issue with particular reference to findings from low resolution structural data. In addition, a number of molecular models of ABCG2 based on high resolution structures of bacterial ABC transporters have recently become available and are critically assessed. ABCG2 is a structurally distinct member of the triumvirate of human multidrug transporters and continues to evade description of a unifying molecular mechanism.

Original languageEnglish
Pages (from-to)57-65
Number of pages9
JournalAdvanced Drug Delivery Reviews
Issue number1
Publication statusPublished - 31 Jan 2009
Externally publishedYes


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