Please use this identifier to cite or link to this item: http://dx.doi.org/10.25673/38658
Title: 3D structure of the transporter ABCG2 : what's new?
Author(s): Eckenstaler, RobertLook up in the Integrated Authority File of the German National Library
Benndorf, RalfLook up in the Integrated Authority File of the German National Library
Issue Date: 2020
Type: Article
Language: English
Abstract: ABCG2 belongs to the ABC transporter superfamily and functions as a poly-specific efflux pump. As it can transport a broad spectrum of substrates out of cells, ABCG2 is thought to alter the pharmacokinetics of drugs applied to treat certain diseases. Especially, its potential to induce resistance to chemotherapy is currently the object of intense research. To foster understanding of mechanisms relevant for substrate recognition and selection of ABCG2 substrates and to finally develop selective therapeutic modulators (e.g. inhibitors) of ABCG2 transport activity, it is important to further explore the precise 3D structure of the transporter. While efforts to elucidate the three-dimensional structure of ABCG2 using X-ray crystal structure analysis have not been successful so far, high-resolution cryo-electron microscopy-based investigations have revealed exciting new insights into the structure and function of the transporter. In this review, we will focus on these seminal publications to summarize the current understanding of tertiary and quaternary structure, homodimerization or oligomerization, and functions of the ABCG2 transporter protein.
URI: https://opendata.uni-halle.de//handle/1981185920/38904
http://dx.doi.org/10.25673/38658
Open Access: Open access publication
License: (CC BY-NC-ND 4.0) Creative Commons Attribution NonCommercial NoDerivatives 4.0(CC BY-NC-ND 4.0) Creative Commons Attribution NonCommercial NoDerivatives 4.0
Sponsor/Funder: Publikationsfond MLU
Journal Title: British journal of pharmacology
Publisher: Wiley
Publisher Place: Malden, MA
Volume: 177
Issue: 7
Original Publication: 10.1111/bph.14991
Page Start: 1485
Page End: 1496
Appears in Collections:Open Access Publikationen der MLU

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