The crystal structure of ORP3 reveals the conservative PI4P binding pattern

Oxysterol-binding protein (OSBP) and its related protein (ORP) constitute a conserved family of lipid transfer proteins (LTPs). ORPs have been implicated as intracellular lipid exchanger and sensor in recent years, which regulate the lipid homeostasis and signal pathway. OSBP-related protein 3 plays...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2020-09, Vol.529 (4), p.1005-1010
Main Authors: Dong, Xue, Wang, Zhiming, Ye, Sheng, Zhang, Rongguang
Format: Article
Language:English
Subjects:
Crystallography, X-Ray
Fatty Acid-Binding Proteins - chemistry
Fatty Acid-Binding Proteins - metabolism
Humans
Models, Molecular
ORP3
OSBP-Related domain
Oxysterol-binding protein
Phosphatidylinositol Phosphates - metabolism
PI4P
Protein Binding
Protein Domains
Structural Homology, Protein
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Summary:Oxysterol-binding protein (OSBP) and its related protein (ORP) constitute a conserved family of lipid transfer proteins (LTPs). ORPs have been implicated as intracellular lipid exchanger and sensor in recent years, which regulate the lipid homeostasis and signal pathway. OSBP-related protein 3 plays key role in controlling cell adhesion and migration and could be developed as the drug target for cancer therapy. Here, we report the crystal structures of human ORP3 ORD to 2.1 Å and ORD-PI4P complex to 3.2 Å. The binding assay in vitro confirms the ORP3 has the capability of PI4P binding. This study further verifies that the PI4P is the common ligand of all ORPs and ORPs should be the lipid exchanger in membrane contact sites(MCS). •The structure of human ORP3 ORD indicates the structure of ORD is well conserved among ORP family.•PI4P is the first ligand of ORP3.
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2020.06.090