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Roles of conserved ectodomain cysteines of the rat P2X4 purinoreceptor in agonist binding and channel gating

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    SYSNO ASEP0355715
    Document TypeJ - Journal Article
    R&D Document TypeJournal Article
    Subsidiary JČlánek ve WOS
    TitleRoles of conserved ectodomain cysteines of the rat P2X4 purinoreceptor in agonist binding and channel gating
    Author(s) Rokic, Milos Boro (FGU-C)
    Tvrdoňová, Vendula (FGU-C)
    Vávra, Vojtěch (FGU-C) RID
    Jindřichová, Marie (FGU-C) RID
    Obšil, T. (CZ)
    Stojilkovic, S. S. (US)
    Zemková, Hana (FGU-C) RID, ORCID
    Source TitlePhysiological Research. - : Fyziologický ústav AV ČR, v. v. i. - ISSN 0862-8408
    Roč. 59, č. 6 (2010), s. 927-935
    Number of pages9 s.
    Languageeng - English
    CountryCZ - Czech Republic
    KeywordsP2X4 receptor ; ATP ; disulfide bonds
    Subject RIVED - Physiology
    R&D ProjectsIAA500110910 GA AV ČR - Academy of Sciences of the Czech Republic (AV ČR)
    GA305/07/0681 GA ČR - Czech Science Foundation (CSF)
    LC554 GA MŠMT - Ministry of Education, Youth and Sports (MEYS)
    CEZAV0Z50110509 - FGU-C (2005-2011)
    UT WOS000285711400010
    AnnotationMammalian P2X receptors contain ten conserved cysteine residues in their ectodomains, which form five disulfide bonds. Replacement of cysteine pairs with threonines resulted in decreased sensitivity of P2X4 receptor to ATP. Three bonds contribute substantially to the structure of the ligand binding pocket, while the bond located towards the transmembrane domain contributes to receptor gating
    WorkplaceInstitute of Physiology
    ContactLucie Trajhanová, lucie.trajhanova@fgu.cas.cz, Tel.: 241 062 400
    Year of Publishing2011
Number of the records: 1  

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