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A Structure-Based View on ABC-Transporter Linked to Multidrug Resistance
The discovery of the first ATP-binding cassette (ABC) transporter, whose overexpression in cancer cells is responsible for exporting anticancer drugs out of tumor cells, initiated enormous efforts to overcome tumor cell multidrug resistance (MDR) by inhibition of ABC-transporter. Because of its many...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9862083/ https://www.ncbi.nlm.nih.gov/pubmed/36677553 http://dx.doi.org/10.3390/molecules28020495 |
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author | Huang, Jiahui Ecker, Gerhard F. |
author_facet | Huang, Jiahui Ecker, Gerhard F. |
author_sort | Huang, Jiahui |
collection | PubMed |
description | The discovery of the first ATP-binding cassette (ABC) transporter, whose overexpression in cancer cells is responsible for exporting anticancer drugs out of tumor cells, initiated enormous efforts to overcome tumor cell multidrug resistance (MDR) by inhibition of ABC-transporter. Because of its many physiological functions, diverse studies have been conducted on the mechanism, function and regulation of this important group of transmembrane transport proteins. In this review, we will focus on the structural aspects of this transporter superfamily. Since the resolution revolution of electron microscope, experimentally solved structures increased rapidly. A summary of the structures available and an overview of recent structure-based studies are provided. More specifically, the artificial intelligence (AI)-based predictions from AlphaFold-2 will be discussed. |
format | Online Article Text |
id | pubmed-9862083 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-98620832023-01-22 A Structure-Based View on ABC-Transporter Linked to Multidrug Resistance Huang, Jiahui Ecker, Gerhard F. Molecules Review The discovery of the first ATP-binding cassette (ABC) transporter, whose overexpression in cancer cells is responsible for exporting anticancer drugs out of tumor cells, initiated enormous efforts to overcome tumor cell multidrug resistance (MDR) by inhibition of ABC-transporter. Because of its many physiological functions, diverse studies have been conducted on the mechanism, function and regulation of this important group of transmembrane transport proteins. In this review, we will focus on the structural aspects of this transporter superfamily. Since the resolution revolution of electron microscope, experimentally solved structures increased rapidly. A summary of the structures available and an overview of recent structure-based studies are provided. More specifically, the artificial intelligence (AI)-based predictions from AlphaFold-2 will be discussed. MDPI 2023-01-04 /pmc/articles/PMC9862083/ /pubmed/36677553 http://dx.doi.org/10.3390/molecules28020495 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Huang, Jiahui Ecker, Gerhard F. A Structure-Based View on ABC-Transporter Linked to Multidrug Resistance |
title | A Structure-Based View on ABC-Transporter Linked to Multidrug Resistance |
title_full | A Structure-Based View on ABC-Transporter Linked to Multidrug Resistance |
title_fullStr | A Structure-Based View on ABC-Transporter Linked to Multidrug Resistance |
title_full_unstemmed | A Structure-Based View on ABC-Transporter Linked to Multidrug Resistance |
title_short | A Structure-Based View on ABC-Transporter Linked to Multidrug Resistance |
title_sort | structure-based view on abc-transporter linked to multidrug resistance |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9862083/ https://www.ncbi.nlm.nih.gov/pubmed/36677553 http://dx.doi.org/10.3390/molecules28020495 |
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