ArticleeLife2022
Structural and functional insights of the human peroxisomal ABC transporter ALDP.
Article in eLife, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 12 citations in OpenAlex.
- Structural basis for LMBD1-dependent trafficking and cobalamin export of ABCD4.Nature communications · 2026Article
- Structural insights into Arabidopsis thaliana CTS-mediated fatty acid and hormone metabolism.Nature communications · 2026Article
- Predictive modelling of the COMATOSE transporter reveals a conserved ligand binding pocket for acyl-CoAs.Scientific reports · 2026Article
- Molecular mechanism of substrate transport by human peroxisomal ABCD3.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- A Novel Missense Variant of the ABCD1 Gene in X-Linked Adrenoleukodystrophy in Chinese Family.Molecular genetics & genomic medicine · 2025Article
- Review
- ATP-Binding Cassette and Solute Carrier Transporters: Understanding Their Mechanisms and Drug Modulation Through Structural and Modeling Approaches.Pharmaceuticals (Basel, Switzerland) · 2024Review
- Structural insights into human ABCD3-mediated peroxisomal acyl-CoA translocation.Cell discovery · 2024Article
- The peroxisome: an update on mysteries 3.0.Histochemistry and cell biology · 2024Review
- Structural basis of substrate recognition and translocation by human very long-chain fatty acid transporter ABCD1.Nature communications · 2022Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Adrenoleukodystrophy protein (ALDP) is responsible for the transport of very-long-chain fatty acids (VLCFAs) and corresponding CoA-esters across the peroxisomal membrane. Dysfunction of ALDP leads to peroxisomal metabolic disorder exemplified by X-linked adrenoleukodystrophy (ALD). Hundreds of ALD-causing mutations have been identified on ALDP. However, the pathogenic mechanisms of these mutations are restricted to clinical description due to limited structural and biochemical characterization. Here we report the cryo-electron microscopy structure of human ALDP with nominal resolution at 3.4 Å. ALDP exhibits a cytosolic-facing conformation. Compared to other lipid ATP-binding cassette transporters, ALDP has two substrate binding cavities formed by the transmembrane domains. Such structural organization may be suitable for the coordination of VLCFAs. Based on the structure, we performed integrative analysis of the cellular trafficking, protein thermostability, ATP hydrolysis, and the transport activity of representative mutations. These results provide a framework for understanding the working mechanism of ALDP and pathogenic roles of disease-associated mutations.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.