The crystal structure of ORP3 reveals the conservative PI4P binding pattern

Xue Dong; Zhiming Wang; Sheng Ye; Rongguang Zhang

doi:10.1016/j.bbrc.2020.06.090

The crystal structure of ORP3 reveals the conservative PI4P binding pattern

Xue Dong
, Zhiming Wang
, Sheng Ye
, Rongguang Zhang^*

^*Corresponding author for this work

Chinese Academy of Sciences

Research output: Contribution to journal › Article › peer-review

13 Scopus citations

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).

Original language	English
Pages (from-to)	1005-1010
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	529
Issue number	4
DOIs	https://doi.org/10.1016/j.bbrc.2020.06.090
State	Published - 3 Sep 2020
Externally published	Yes

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

Keywords

ORP3
OSBP-Related domain
Oxysterol-binding protein
PI4P

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10.1016/j.bbrc.2020.06.090

Cite this

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title = "The crystal structure of ORP3 reveals the conservative PI4P binding pattern",

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 {\AA} and ORD-PI4P complex to 3.2 {\AA}. 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).",

keywords = "ORP3, OSBP-Related domain, Oxysterol-binding protein, PI4P",

author = "Xue Dong and Zhiming Wang and Sheng Ye and Rongguang Zhang",

note = "Publisher Copyright: {\textcopyright} 2020 Elsevier Inc.",

year = "2020",

month = sep,

day = "3",

doi = "10.1016/j.bbrc.2020.06.090",

language = "英语",

volume = "529",

pages = "1005--1010",

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}

TY - JOUR

T1 - The crystal structure of ORP3 reveals the conservative PI4P binding pattern

AU - Dong, Xue

AU - Wang, Zhiming

AU - Ye, Sheng

AU - Zhang, Rongguang

PY - 2020/9/3

Y1 - 2020/9/3

N2 - 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).

AB - 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).

KW - ORP3

KW - OSBP-Related domain

KW - Oxysterol-binding protein

KW - PI4P

UR - https://www.scopus.com/pages/publications/85088791053

U2 - 10.1016/j.bbrc.2020.06.090

DO - 10.1016/j.bbrc.2020.06.090

M3 - 文章

C2 - 32819557

AN - SCOPUS:85088791053

SN - 0006-291X

VL - 529

SP - 1005

EP - 1010

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 4

ER -

The crystal structure of ORP3 reveals the conservative PI4P binding pattern

Abstract

UN SDGs

Keywords

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