Structure and mechanism of ABC transporters
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Updated: Sep 28, 2026

ABCG5/G8 Crystallization in a Lipidic Bicelle Environment for X-Ray Crystallography
Published on: August 25, 2023
1Institute of Biochemistry, Biocenter, Goethe-University Frankfurt, Marie-Curie Strasse 9, Germany. lschmitt@em.uni-frankfurt.de
Abstract:
ATP-binding cassette (ABC) transporters are central to many physiological processes, including the uptake of nutrients, the non-classical secretion of signaling molecules and toxins, multidrug resistance and the development of human disease. As one might expect from this spectrum of translocation events, these ubiquitous, ATP-dependent pumps or channels are capable of transporting an enormous variety of substrates, ranging from small ions to large proteins. Recently determined structures of full-length ABC transporters and isolated ABC domains have increased our understanding of the functional mechanism of these proteins.
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