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Crystal Structure of the ORP8 Lipid Transport ORD Domain: Model of Lipid Transport

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F23%3A00574877" target="_blank" >RIV/61388963:_____/23:00574877 - isvavai.cz</a>

  • Result on the web

    <a href="https://doi.org/10.3390/cells12151974" target="_blank" >https://doi.org/10.3390/cells12151974</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.3390/cells12151974" target="_blank" >10.3390/cells12151974</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Crystal Structure of the ORP8 Lipid Transport ORD Domain: Model of Lipid Transport

  • Original language description

    ORPs are lipid-transport proteins belonging to the oxysterol-binding protein family. They facilitate the transfer of lipids between different intracellular membranes, such as the ER and plasma membrane. We have solved the crystal structure of the ORP8 lipid transport domain (ORD8). The ORD8 exhibited a β-barrel fold composed of anti-parallel β-strands, with three α-helices replacing β-strands on one side. This mixed alpha–beta structure was consistent with previously solved structures of ORP2 and ORP3. A large cavity (≈1860 Å3) within the barrel was identified as the lipid-binding site. Although we were not able to obtain a lipid-bound structure, we used computer simulations based on our crystal structure to dock PS and PI4P molecules into the putative lipid-binding site of the ORD8. Comparative experiments between the short ORD8ΔLid (used for crystallography) and the full-length ORD8 (lid containing) revealed the lid’s importance for stable lipid binding. Fluorescence assays revealed different transport efficiencies for PS and PI4P, with the lid slowing down transport and stabilizing cargo. Coarse-grained simulations highlighted surface-exposed regions and hydrophobic interactions facilitating lipid bilayer insertion. These findings enhance our comprehension of ORD8, its structure, and lipid transport mechanisms, as well as provide a structural basis for the design of potential inhibitors.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10608 - Biochemistry and molecular biology

Result continuities

  • Project

    <a href="/en/project/GF21-27735K" target="_blank" >GF21-27735K: Structural and functional analysis of regulation of the lipid-transport protein ORP8</a><br>

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2023

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Cells

  • ISSN

    2073-4409

  • e-ISSN

    2073-4409

  • Volume of the periodical

    12

  • Issue of the periodical within the volume

    15

  • Country of publishing house

    CH - SWITZERLAND

  • Number of pages

    13

  • Pages from-to

    1974

  • UT code for WoS article

    001046164200001

  • EID of the result in the Scopus database

    2-s2.0-85167626631