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J. Biol. Chem., Vol. 282, Issue 27, 19526-19533, July 6, 2007

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A Histidine Scan to Probe the Flexibility of the Rat P2X₂ Receptor Zinc-binding Site^*

From the Department of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, Michigan 48109-1048

The response of P2X₂ receptors to submaximal concentrations of ATP is potentiated by low levels of extracellular zinc. Histidines 120 and 213 have previously been shown to be essential in binding zinc across an intersubunit binding site. We tested the flexibility of the zinc-binding site by making mutations that had the effect of shifting the two essential histidines up to 13 residues upstream or downstream from their original positions and then testing the ability of the mutated receptors to respond to zinc. Using this method, we were able to explore potential orientations of the two regions relative to one another. Our data are consistent with a moderately flexible zinc-binding site and inconsistent with parallel and anti-parallel orientations of the regions surrounding histidines 120 and 213.

Received for publication, February 23, 2007 , and in revised form, May 3, 2007.

^* This work was supported by National Institutes of Health Grants R01-NS039196 (to R. I. H.) and F31-NS051001 (to R. K. T.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed: Dept. of Molecular, Cellular, and Developmental Biology, 830 North University Ave., Ann Arbor, MI 48109-1048. Tel.: 734-764-7427; Fax: 734-615-6337; E-mail: rhume{at}umich.edu.

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