7CYZ

The structure of human ORP3 OSBP-related domain

Summary for 7CYZ

• Entry DOI: 10.2210/pdb7cyz/pdb
• Descriptor: Oxysterol-binding protein-related protein 3 (2 entities in total)
• Functional Keywords: lipid transfer protein, lipid binding protein, osbp related protein
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 2
• Total formula weight: 88648.97

Authors

Dong, X. (deposition date: 2020-09-05, release date: 2020-10-28, Last modification date: 2024-10-09)

Primary citation

Dong, X.,Wang, Z.,Ye, S.,Zhang, R.
The crystal structure of ORP3 reveals the conservative PI4P binding pattern.
Biochem.Biophys.Res.Commun., 529:1005-1010, 2020

PubMed Abstract: 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).

PubMed: 32819557
DOI: 10.1016/j.bbrc.2020.06.090

Experimental method

X-RAY DIFFRACTION (2.1 Å)