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https://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 |
DOI: | 10.1016/j.str.2006.08.014 |
Published version: | http://dx.doi.org/10.1016/j.str.2006.08.014 |
Appears in Collections: | Aurora harvest 5 Molecular and Biomedical Science publications |
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