ArticleCells2023
Crystal Structure of the ORP8 Lipid Transport ORD Domain: Model of Lipid Transport.
Article in Cells, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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Who cites it
4 citing papers in PubMed.
- Phosphatidylinositol transfer protein α binds microcolins in its open conformation.Acta crystallographica. Section D, Structural biology · 2026Article
- Endoplasmic reticulum-mitochondria crosstalk: new mechanisms in the development of atherosclerosis.Frontiers in endocrinology · 2025Review
- Lysosomal membrane contact sites: Integrative hubs for cellular communication and homeostasis.Current topics in membranes · 2024Review
- Getting to Grips with the Oxysterol-Binding Protein Family - a Forty Year Perspective.Contact (Thousand Oaks (Ventura County, Calif.))Review
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
ORPs are lipid-transport proteins belonging to the oxysterol-binding protein family. They facilitate the transfer of lipids between different intracellular membranes, such as the ER and plasma membrane. We have solved the crystal structure of the ORP8 lipid transport domain (ORD8). The ORD8 exhibited a β-barrel fold composed of anti-parallel β-strands, with three α-helices replacing β-strands on one side. This mixed alpha-beta structure was consistent with previously solved structures of ORP2 and ORP3. A large cavity (≈1860 Å
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