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The pi-helix formation between Asp(369) and Thr(375) as a key factor in E(1)-E(2) conformational change of Na(+)/K(+)-ATPase

  1. 1.
    SYSNO ASEP0318424
    Document TypeJ - Journal Article
    R&D Document TypeJournal Article
    Subsidiary JČlánek ve WOS
    TitleThe pi-helix formation between Asp(369) and Thr(375) as a key factor in E(1)-E(2) conformational change of Na(+)/K(+)-ATPase
    TitleVznik π-helixu mezi Asp369–Thr375 je klíčový pro E1-E2 konformační změnu Na+/K+-ATPázy
    Author(s) Tejral, Gracian (UEM-P)
    Koláčná, Lucie (UEM-P)
    Schoner, W. (DE)
    Amler, Evžen (UEM-P) RID
    Source TitlePhysiological Research. - : Fyziologický ústav AV ČR, v. v. i. - ISSN 0862-8408
    Roč. 58, č. 4 (2009), s. 583-589
    Number of pages7 s.
    Languageeng - English
    CountryCZ - Czech Republic
    Keywordscomputer modeling ; molecular dynamics simulations ; molecular structure
    Subject RIVBO - Biophysics
    R&D Projects1ET400110403 GA AV ČR - Academy of Sciences of the Czech Republic (AV ČR)
    IAA500390702 GA AV ČR - Academy of Sciences of the Czech Republic (AV ČR)
    2B06130 GA MŠMT - Ministry of Education, Youth and Sports (MEYS)
    GA202/09/1151 GA ČR - Czech Science Foundation (CSF)
    CEZAV0Z50390512 - UEM-P (2005-2011)
    AV0Z50390703 - UEM-P (2007-2013)
    UT WOS000270857000014
    DOIdoi:10.1186/1472-6750-8-70
    AnnotationH4-H5-loop structure of Na+/K+-ATPase in E1 and E2 conformations was studied by molecular modeling. E1-E2 transition is connected with π-helix formation (Asp369–Thr375) and distance-shortening between the ATP binding and phosphorylation site by 1.22 nm.
    WorkplaceInstitute of Experimental Medicine
    ContactLenka Koželská, lenka.kozelska@iem.cas.cz, Tel.: 241 062 218, 296 442 218
    Year of Publishing2010
Number of the records: 1  

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