Molecular assembly of the extracellular domain of P2X(2) an ATP-gated ion channel

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We have produced the putative extracellular domain (ECD) of the ATP-gated ion channel, P2X(2), in a bacterial expression system. The hexahistidine-tagged protein was purified by immobilized metal affinity chromatography and refolded by sulfitolysis and dialysis. We demonstrate that P2X(2)-ECD forms a stable tetramer in solution by gel filtration chromatography, dynamic light scattering and analytical sedimentation centrifugation. [alpha-P-32]ATP has been covalently cross-linked by UV irradiation to the P2X(2)-ECD and this binding is specific and competable by antagonists suramin and cibacron blue. These results indicate that the binding affinity among P2X(2)-ECD subunits is appreciably stronger than 3.4 mu M (0.1 mg/ml), implying that the extracellular domain of P2X(2) is primarly responsible for tetramerization of whole P2X(2) and thus probably plays a role in determining home-and heteromerization specificity of P2X channel subunits. (C) 1997 Academic Press.
Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
Issue Date
1997-09
Language
English
Article Type
Article
Keywords

FUNCTIONAL EXPRESSION; POTASSIUM CHANNEL; SENSORY NEURONS; P-2X RECEPTOR; PURINOCEPTORS; CLONING; SUBUNITS; BRAIN

Citation

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.240, no.3, pp.618 - 622

ISSN
0006-291X
URI
http://hdl.handle.net/10203/77675
Appears in Collection
MSE-Journal Papers(저널논문)
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