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Roles of conserved ectodomain cysteines of the rat P2X4 purinoreceptor in agonist binding and channel gating
- 1.0355715 - FGÚ 2011 RIV CZ eng J - Journal Article
Rokic, Milos Boro - Tvrdoňová, Vendula - Vávra, Vojtěch - Jindřichová, Marie - Obšil, T. - Stojilkovic, S. S. - Zemková, Hana
Roles of conserved ectodomain cysteines of the rat P2X4 purinoreceptor in agonist binding and channel gating.
Physiological Research. Roč. 59, č. 6 (2010), s. 927-935. ISSN 0862-8408. E-ISSN 1802-9973
R&D Projects: GA AV ČR(CZ) IAA500110910; GA ČR(CZ) GA305/07/0681; GA MŠMT(CZ) LC554
Institutional research plan: CEZ:AV0Z50110509
Keywords : P2X4 receptor * ATP * disulfide bonds
Subject RIV: ED - Physiology
Impact factor: 1.646, year: 2010
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
Permanent Link: http://hdl.handle.net/11104/0194417
Number of the records: 1