Journal
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
Volume 1860, Issue 4, Pages 818-832Publisher
ELSEVIER
DOI: 10.1016/j.bbamem.2017.10.028
Keywords
ABC transporter; ABCB1; P-glycoprotein; Molecular dynamics simulations; Transport cycle; Mechanistic models
Categories
Funding
- Austrian Science Fund (FWF) [P23319]
- SFB [F3524]
- Carl-Zeiss Foundation
- Center of Biomolecular Magnetic Resonance (BMRZ) - state of Hesse
- Fulbright-Cottrell Award - German-American Fulbright commission
- Fulbright-Cottrell Award - Research Corporation for Science Advancement (RCSA)
- Fulbright-Cottrell Award - Bundesministerium fur Bildung and Forschung (BMBF)
- Hans Bockler Stiftung
- Austrian Science Fund (FWF) [P23319] Funding Source: Austrian Science Fund (FWF)
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ABC (ATP binding cassette) transporters, ubiquitous in all kingdoms of life, carry out essential substrate transport reactions across cell membranes. Their transmembrane domains bind and translocate substrates and are connected to a pair of nucleotide binding domains, which bind and hydrolyze ATP to energize import or export of substrates. Over four decades of investigations into ABC transporters have revealed numerous details from atomic-level structural insights to their functional and physiological roles. Despite all these advances, a comprehensive understanding of the mechanistic principles of ABC transporter function remains elusive. The human multidrug resistance transporter ABCB1, also referred to as P-glycoprotein (P-gp), is one of the most intensively studied ABC exporters. Using ABCB1 as the reference point, we aim to compare the dominating mechanistic models of substrate transport and ATP hydrolysis for ABC exporters and to highlight the experimental and computational evidence in their support. In particular, we point out in silico studies that enhance and complement available biochemical data. This article is part of a Special Issue entitled: Beyond the Structure Function Horizon of Membrane Proteins edited by Ute Hellmich, Rupak Doshi and Benjamin Mcllwain.
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