Please use this identifier to cite or link to this item: http://hdl.handle.net/2381/15561
Title: Conserved negatively charged residues are not required for ATP action at P2X(1) receptors.
Authors: Ennion, SJ
Ritson, J
Evans, RJ
First Published: 7-Dec-2001
Citation: BIOCHEM BIOPHYS RES COMMUN, 2001, 289 (3), pp. 700-704
Abstract: The role of conserved negatively charged aspartic (D) and glutamic (E) acid residues within the ectodomain of the human P2X(1) receptor were examined by alanine substitution mutagenesis. Effects on ATP potency and cell surface localisation were assessed in Xenopus oocytes using the two electrode voltage clamp technique and cell surface biotinylation. Of the eleven residues tested no major shifts in ATP potency were observed with EC(50) values for ATP ranging from 0.8 to 4.3 microM (compared to 1 microM ATP for wild-type P2X(1) receptors). Peak current amplitudes for mutants D86A and D264A where reduced by approximately 90% due to a corresponding reduction in both total protein and cell surface expression. These results demonstrate that individual conserved negatively charged amino acids are not essential for ATP recognition by the human P2X(1) receptor and coordinated binding of the positive charge on magnesium complexed ATP by negatively charged amino acids is not required.
DOI Link: 10.1006/bbrc.2001.6034
ISSN: 0006-291X
Links: http://hdl.handle.net/2381/15561
Type: Journal Article
Appears in Collections:Published Articles, Dept. of Cell Physiology and Pharmacology

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