Abstract
1. 5-Hydroxytryptamine (10 microM) enhanced ionic current mediated through the wild-type P2X2 receptor/channel expressed in Xenopus oocytes. 2. 5-Hydroxytryptamine (10 microM) inhibited a current mediated through P2X2 receptor/channel mutants when Thr330 or Asn333 was replaced with Ile (T330I and N333I). 3. Our results suggest that neutralization of Thr330 or Asn333 exposes a high-affinity, inhibitory binding site for 5-hydroxytryptamine. This implies that 5-hydroxytryptamine interacts with the P2X2 receptor/channel at their channel pores.
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