Abstract 2363 Probing the function of the 265-290 loop of perilipin 5
Central to numerous modern health concerns is excessive or aberrant lipid storage. Nearly all cells store neutral lipids in organelles termed lipid storage droplets. Perilipin 5 is a lipid storage droplet protein with several established roles in triacylglycerol metabolism. The perilipin 5 sequence is highly conserved with perilipin 3 and both are thought to share several important structural features. One of these is a four-helix bundle with a mixed alpha-beta structure which resembles a boot. At the top of the four-helix bundle is a short loop structure we have termed the 265-290 loop.
Authors
- John T. Tansey (ORCID: https://orcid.org/0000-0002-1288-6473)
- Kenneth V. Snyder (ORCID: https://orcid.org/0000-0002-0842-9026)
- Seethalakshmi Iyer
- Nicholas Manivilovski
Institutions
- Bridge University (SS)
Publication Details
- Journal
- Journal of Biological Chemistry
- Published
- 2025-05-01
- DOI
- https://doi.org/10.1016/j.jbc.2025.109429
- Primary Topic
- DNA and Nucleic Acid Chemistry
- Type
- article
- Field-Weighted Citation Impact
- 0.00