Počet záznamů: 1  

Molecular dynamics simulations of mitochondrial uncoupling protein 2

  1. 1.
    SYSNO ASEP0539523
    Druh ASEPJ - Článek v odborném periodiku
    Zařazení RIVJ - Článek v odborném periodiku
    Poddruh JČlánek ve WOS
    NázevMolecular dynamics simulations of mitochondrial uncoupling protein 2
    Tvůrce(i) Škulj, S. (HR)
    Brkljača, Z. (HR)
    Kreiter, J. (AT)
    Pohl, E. E. (AT)
    Vazdar, Mario (UOCHB-X) ORCID
    Číslo článku1214
    Zdroj.dok.International Journal of Molecular Sciences. - : MDPI
    Roč. 22, č. 3 (2021)
    Poč.str.20 s.
    Jazyk dok.eng - angličtina
    Země vyd.CH - Švýcarsko
    Klíč. slovamembrane protein ; long-chain fatty acid ; proton transfer ; purine nucleotide ; conductance measurements in model membranes ; uncoupling
    Obor OECDPhysical chemistry
    Způsob publikováníOpen access
    Institucionální podporaUOCHB-X - RVO:61388963
    UT WOS000615325400001
    EID SCOPUS85099936405
    DOI10.3390/ijms22031214
    AnotaceMolecular dynamics (MD) simulations of uncoupling proteins (UCP), a class of transmembrane proteins relevant for proton transport across inner mitochondrial membranes, represent a complicated task due to the lack of available structural data. In this work, we use a combination of homology modelling and subsequent microsecond molecular dynamics simulations of UCP2 in the DOPC phospholipid bilayer, starting from the structure of the mitochondrial ATP/ADP carrier (ANT) as a template. We show that this protocol leads to a structure that is impermeable to water, in contrast to MD simulations of UCP2 structures based on the experimental NMR structure. We also show that ATP binding in the UCP2 cavity is tight in the homology modelled structure of UCP2 in agreement with experimental observations. Finally, we corroborate our results with conductance measurements in model membranes, which further suggest that the UCP2 structure modeled from ANT protein possesses additional key functional elements, such as a fatty acid-binding site at the R60 region of the protein, directly related to the proton transport mechanism across inner mitochondrial membranes.
    PracovištěÚstav organické chemie a biochemie
    Kontaktasep@uochb.cas.cz ; Kateřina Šperková, Tel.: 232 002 584 ; Viktorie Chládková, Tel.: 232 002 434
    Rok sběru2022
    Elektronická adresahttps://doi.org/10.3390/ijms22031214
Počet záznamů: 1  

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