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The spider peptide toxin psalmotoxin 1 (PcTx1) has previously been shown to inhibit specifically the proton\u2010gated cation channel ASIC1a. To identify the binding site of PcTx1, we produced an iodinated form of the toxin (<jats:sup>125<\/jats:sup>I\u2010PcTx1Y<jats:sub>N<\/jats:sub>) and developed a set of binding and electrophysiological experiments on several chimeras of ASIC1a and the PcTx1\u2010insensitive channels ASIC1b and ASIC2a. We show that <jats:sup>125<\/jats:sup>I\u2010PcTx1Y<jats:sub>N<\/jats:sub> binds specifically to ASIC1a at a single site, with an IC<jats:sub>50<\/jats:sub> of 128 p<jats:sc>m<\/jats:sc>, distinct from the amiloride blocking site. Results obtained from chimeras indicate that PcTx1 does not bind to ASIC1a transmembrane domains (M1 and M2), involved in formation of the ion pore, but binds principally on both cysteine\u2010rich domains I and II (CRDI and CRDII) of the extracellular loop. The post\u2010M1 and pre\u2010M2 regions, although not involved in the binding site, are crucial for the ability of PcTx1 to inhibit ASIC1a current. The linker domain between CRDI and CRDII is important for their correct spatial positioning to form the PcTx1 binding site. 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