A putative extracellular salt bridge at the subunit interface contributes to the ion channel function of the ATP-gated P2X2 receptor.
Jiang
Ruotian
R
Laboratoire de Biophysicochimie des Récepteurs Canaux, UMR 7199 CNRS, Conception et Application de Molécules Bioactives, Faculté de Pharmacie, Université de Strasbourg, 74 route du Rhin, BP 24, 67401 Illkirch Cedex, France.
Martz
Adeline
A
Gonin
Sophie
S
Taly
Antoine
A
de Carvalho
Lia Prado
LP
Grutter
Thomas
T
D000255:Adenosine Triphosphate / Q000737:chemistry / Q000378:metabolism*; D019943:Amino Acid Substitution; D000818:Animals; D002460:Cell Line; D004220:Disulfides / Q000378:metabolism; D006801:Humans; D015640:Ion Channel Gating / Q000502:physiology*; D020125:Mutation, Missense; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D021122:Protein Subunits / Q000235:genetics / Q000378:metabolism; D051381:Rats; D018048:Receptors, Purinergic P2 / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D058476:Receptors, Purinergic P2X2
D004220:Disulfides; C546401:P2RX2 protein, human; D021122:Protein Subunits; D018048:Receptors, Purinergic P2; D058476:Receptors, Purinergic P2X2; D000255:Adenosine Triphosphate