Next Article in Journal
Application of Extrusion-Based Hydrogel Bioprinting for Cartilage Tissue Engineering
Next Article in Special Issue
Increased Expression of Plasma-Induced ABCC1 mRNA in Cystic Fibrosis
Previous Article in Journal
The Role of p16INK4a Pathway in Human Epidermal Stem Cell Self-Renewal, Aging and Cancer
Previous Article in Special Issue
ABCC6 and Pseudoxanthoma Elasticum: The Face of a Rare Disease from Genetics to Advocacy
Article Menu
Issue 7 (July) cover image

Export Article

Open AccessArticle
Int. J. Mol. Sci. 2017, 18(7), 1593;

Predictive Structure and Topology of Peroxisomal ATP-Binding Cassette (ABC) Transporters

Laboratoire Bio-PeroxIL EA7270, University of Bourgogne Franche-Comté, 6 Bd Gabriel, 21000 Dijon, France
Authors to whom correspondence should be addressed.
Received: 26 June 2017 / Revised: 10 July 2017 / Accepted: 19 July 2017 / Published: 22 July 2017
(This article belongs to the Special Issue Physiological and Pathological Roles of ABC Transporters)
Full-Text   |   PDF [3264 KB, uploaded 22 July 2017]   |  


The peroxisomal ATP-binding Cassette (ABC) transporters, which are called ABCD1, ABCD2 and ABCD3, are transmembrane proteins involved in the transport of various lipids that allow their degradation inside the organelle. Defective ABCD1 leads to the accumulation of very long-chain fatty acids and is associated with a complex and severe neurodegenerative disorder called X-linked adrenoleukodystrophy (X-ALD). Although the nucleotide-binding domain is highly conserved and characterized within the ABC transporters family, solid data are missing for the transmembrane domain (TMD) of ABCD proteins. The lack of a clear consensus on the secondary and tertiary structure of the TMDs weakens any structure-function hypothesis based on the very diverse ABCD1 mutations found in X-ALD patients. Therefore, we first reinvestigated thoroughly the structure-function data available and performed refined alignments of ABCD protein sequences. Based on the 2.85  Å resolution crystal structure of the mitochondrial ABC transporter ABCB10, here we propose a structural model of peroxisomal ABCD proteins that specifies the position of the transmembrane and coupling helices, and highlight functional motifs and putative important amino acid residues. View Full-Text
Keywords: ATP-binding Cassette (ABC) transporters; peroxisome; fatty acid transport; topology; predictive structure; adrenoleukodystrophy ATP-binding Cassette (ABC) transporters; peroxisome; fatty acid transport; topology; predictive structure; adrenoleukodystrophy

Graphical abstract

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

Supplementary material


Share & Cite This Article

MDPI and ACS Style

Andreoletti, P.; Raas, Q.; Gondcaille, C.; Cherkaoui-Malki, M.; Trompier, D.; Savary, S. Predictive Structure and Topology of Peroxisomal ATP-Binding Cassette (ABC) Transporters. Int. J. Mol. Sci. 2017, 18, 1593.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics



[Return to top]
Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top