Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/54738
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Type: Journal article
Title: Purification and 3-D structural analysis of oligomeric human multidrug transporter ABCG2
Author: McDevitt, C.
Collins, R.
Conway, M.
Modok, S.
Storm, J.
Kerr, I.
Ford, R.
Callaghan, R.
Citation: Structure, 2006; 14(11):1623-1632
Publisher: Cell Press
Issue Date: 2006
ISSN: 0969-2126
1878-4186
Statement of
Responsibility: 
Christopher A. McDevitt, Richard F. Collins, Michael Conway, Szabolcs Modok, Janet Storm, Ian D. Kerr, Robert C. Ford and Richard Callaghan
Abstract: ABCG2 is a multidrug efflux pump associated with resistance of cancer cells to a plethora of unrelated drugs. ABCG2 is a “half-transporter,” and previous studies have indicated that it forms homodimers and higher oligomeric species. In this manuscript, electron microscopic structural analysis directly addressed this issue. An N-terminal hexahistidine-tagged ABCG2R482G isoform was expressed to high levels in insect cells. An extensive detergent screen was employed to effect extraction of ABCG2R482G from membranes and identified only the fos-choline detergents as efficient. Soluble protein was purified to >95% homogeneity by a three-step procedure while retaining the ability to bind substrates. Cryonegative stain electron microscopy of purified ABCG2R482G provided 3D structural data at a resolution of 18 Å. Single-particle analysis revealed that the complex forms a tetrameric complex (180 Å in diameter × 140 Å high) with an aqueous central region. We interpret the tetrameric structure as comprising four homodimeric ABCG2R482G complexes.
Keywords: Cellbio; Cellcycle
RMID: 0020093535
DOI: 10.1016/j.str.2006.08.014
Appears in Collections:Molecular and Biomedical Science publications

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