{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,9,23]],"date-time":"2025-09-23T14:16:40Z","timestamp":1758637000576},"reference-count":47,"publisher":"Wiley","issue":"9","license":[{"start":{"date-parts":[[2009,1,1]],"date-time":"2009-01-01T00:00:00Z","timestamp":1230768000000},"content-version":"vor","delay-in-days":1949,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Protein Science"],"published-print":{"date-parts":[[2003,9]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Pi4 is a short toxin found at very low abundance in the venom of <jats:italic>Pandinus imperator<\/jats:italic> scorpions. It is a potent blocker of K<jats:sup>+<\/jats:sup> channels. Like the other members of the \u03b1\u2010KTX6 subfamily to which it belongs, it is cross\u2010linked by four disulfide bonds. The synthetic analog (sPi4) and the natural toxin (nPi4) have been obtained by solid\u2010phase synthesis or from scorpion venom, respectively. Analysis of two\u2010dimensional <jats:sup>1<\/jats:sup>H NMR spectra of nPi4 and sPi4 indicates that both peptides have the same structure. Moreover, electrophysiological recordings of the blocking of Shaker B K<jats:sup>+<\/jats:sup> channels by sPi4 (K<jats:sub>D<\/jats:sub> = 8.5 nM) indicate that sPi4 has the same blocking activity of nPi4 (K<jats:sub>D<\/jats:sub> = 8.0 nM), previously described. The disulfide bonds have been independently determined by NMR and structure calculations, and by Edman\u2010degradation\/mass\u2010spectrometry identification of peptides obtained by proteolysis of nPi4. Both approaches indicate that the pairing of the half\u2010cystines is <jats:sup>6<\/jats:sup>C\u2013<jats:sup>27<\/jats:sup>C, <jats:sup>12<\/jats:sup>C\u2013<jats:sup>32<\/jats:sup>C, <jats:sup>16<\/jats:sup>C\u2013<jats:sup>34<\/jats:sup>C, and <jats:sup>22<\/jats:sup>C\u2013<jats:sup>37<\/jats:sup>C. The structure of the toxin has been determined by using 705 constraints derived from NMR data on sPi4. The structure, which is well defined, shows the characteristic \u03b1\/\u03b2 scaffold of scorpion toxins. It is compared to the structure of the other \u03b1\u2010KTX6 subfamily members and, in particular, to the structure of maurotoxin, which shows a different pattern of disulfide bridges despite its high degree of sequence identity (76%) with Pi4. The structure of Pi4 and the high amounts of synthetic peptide available, will enable the detailed analysis of the interaction of Pi4 with K<jats:sup>+<\/jats:sup> channels.<\/jats:p>","DOI":"10.1110\/ps.03186703","type":"journal-article","created":{"date-parts":[[2003,8,27]],"date-time":"2003-08-27T22:42:05Z","timestamp":1062024125000},"page":"1844-1854","source":"Crossref","is-referenced-by-count":11,"title":["Solution structure of Pi4, a short four\u2010disulfide\u2010bridged scorpion toxin specific of potassium channels"],"prefix":"10.1002","volume":"12","author":[{"given":"J. I\u00f1aki","family":"Guijarro","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sarrah","family":"M'Barek","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Froylan","family":"G\u00f3mez\u2010Lagunas","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Damien","family":"Garnier","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Herv\u00e9","family":"Rochat","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jean\u2010Marc","family":"Sabatier","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Lourrival 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