7cyz
From Proteopedia
The structure of human ORP3 OSBP-related domain
Structural highlights
Publication Abstract from PubMedOxysterol-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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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