7cyz

The structure of human ORP3 OSBP-related domain

spinqualitylabelsall models 7cyz, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.1Å Ligands: CAF Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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 A and ORD-PI4P complex to 3.2 A. 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 crystal structure of ORP3 reveals the conservative PI4P binding pattern.,Dong X, Wang Z, Ye S, Zhang R Biochem Biophys Res Commun. 2020 Sep 3;529(4):1005-1010. doi:, 10.1016/j.bbrc.2020.06.090. Epub 2020 Jul 30. PMID:32819557 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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