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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 ASEP 0355715 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Roles 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, ORCIDSource Title Physiological Research. - : Fyziologický ústav AV ČR, v. v. i. - ISSN 0862-8408
Roč. 59, č. 6 (2010), s. 927-935Number of pages 9 s. Language eng - English Country CZ - Czech Republic Keywords P2X4 receptor ; ATP ; disulfide bonds Subject RIV ED - Physiology R&D Projects IAA500110910 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) CEZ AV0Z50110509 - FGU-C (2005-2011) UT WOS 000285711400010 Annotation Mammalian 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 Workplace Institute of Physiology Contact Lucie Trajhanová, lucie.trajhanova@fgu.cas.cz, Tel.: 241 062 400 Year of Publishing 2011
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