Structure of human phospholipase <scp>D</scp>3, a single‐strand exonuclease associated with Alzheimer's disease
Phospholipase D3 (PLD3) has emerged as an important 5'-exonuclease in charge of removing single-stranded DNA in lysosomes. Rare genetic variants of the gene encoding PLD3 have been implicated in late-onset Alzheimer's disease (AD). Ishii et al. have produced the soluble domain of human PLD3 with the aim of determining its three-dimensional structure using X-ray crystallography. The high-resolution structure (2.3 Å) provides new insights into the biochemical properties of the enzyme and paves the way to a deeper understanding of amino acid replacements affecting the stability and activity of the enzyme.
Authors
- Aleksandar Bijelic (ORCID: https://orcid.org/0000-0002-8781-153X)
- Peter Macheroux (ORCID: https://orcid.org/0000-0002-0242-454X)
Institutions
- Graz University of Technology (AT)
Publication Details
- Journal
- FEBS Journal
- Published
- 2024-11-08
- DOI
- https://doi.org/10.1111/febs.17319
- Primary Topic
- Genetics and Neurodevelopmental Disorders
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- TU Graz, Internationale Beziehungen und Mobilitätsprogramme