{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,26]],"date-time":"2025-10-26T22:44:54Z","timestamp":1761518694612},"reference-count":37,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2009,4,13]],"date-time":"2009-04-13T00:00:00Z","timestamp":1239580800000},"content-version":"vor","delay-in-days":2628,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Protein Science"],"published-print":{"date-parts":[[2002,2]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>A new K<jats:sup>+<\/jats:sup>\u2010channel blocking peptide identified from the scorpion venom of <jats:italic>Tityus cambridgei<\/jats:italic> (Tc1) is composed of 23 amino acid residues linked with three disulfide bridges. Tc1 is the shortest known toxin from scorpion venom that recognizes the <jats:italic>Shaker<\/jats:italic> B K<jats:sup>+<\/jats:sup> channels and the voltage\u2010dependent K<jats:sup>+<\/jats:sup> channels in the brain. Synthetic Tc1 was produced using solid\u2010phase synthesis, and its activity was found to be the same as that of native Tc1. The pairings of three disulfide bridges in the synthetic Tc1 were identified by NMR experiments. The NMR solution structures of Tc1 were determined by simulated annealing and energy\u2010minimization calculations using the X\u2010PLOR program. The results showed that Tc1 contains an \u03b1\u2010helix and a 3<jats:sub>10<\/jats:sub>\u2010helix at N\u2010terminal Gly<jats:sup>4<\/jats:sup>\u2013Lys<jats:sup>10<\/jats:sup> and a double\u2010stranded \u03b2\u2010sheet at Gly<jats:sup>13<\/jats:sup>\u2013Ile<jats:sup>16<\/jats:sup> and Arg<jats:sup>19<\/jats:sup>\u2013Tyr<jats:sup>23<\/jats:sup>, with a type I\u2032 \u03b2\u2010turn at Asn<jats:sup>17<\/jats:sup>\u2013Gly<jats:sup>18<\/jats:sup>. Superposition of each structure with the best structure yielded an average root mean square deviation of 0.26 \u00b1 0.05 \u00c5 for the backbone atoms and of 1.40 \u00b1 0.23 \u00c5 for heavy atoms in residues 2 to 23. The three\u2010dimensional structure of Tc1 was compared with two structurally and functionally related scorpion toxins, charybdotoxin (ChTx) and noxiustoxin (NTx). We concluded that the C\u2010terminal structure is the most important region for the blocking activity of voltage\u2010gated (Kv\u2010type) channels for scorpion K<jats:sup>+<\/jats:sup>\u2010channel blockers. We also found that some of the residues in the larger scorpion K<jats:sup>+<\/jats:sup>\u2010channel blockers (31 to 40 amino acids) are not involved in K<jats:sup>+<\/jats:sup>\u2010channel blocking activity.<\/jats:p>","DOI":"10.1110\/ps.33402","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T23:59:58Z","timestamp":1027727998000},"page":"390-400","source":"Crossref","is-referenced-by-count":13,"title":["Solution structure of a K<sup>+<\/sup>\u2010channel blocker from the scorpion <i>Tityus cambridgei<\/i>"],"prefix":"10.1002","volume":"11","author":[{"given":"Iren","family":"Wang","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Shih\u2010Hsiung","family":"Wu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Hsueh\u2010Kai","family":"Chang","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ru\u2010Chi","family":"Shieh","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Hui\u2010Ming","family":"Yu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Chinpan","family":"Chen","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2009,4,13]]},"reference":[{"key":"e_1_2_7_2_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0014-5793(00)02253-5"},{"key":"e_1_2_7_3_1","doi-asserted-by":"publisher","DOI":"10.1016\/0022-2364(85)90018-6"},{"key":"e_1_2_7_4_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1432-1033.1991.tb15780.x"},{"key":"e_1_2_7_5_1","volume-title":"X\u2010PLOR version 98","author":"Br\u00fcnger A.T.","year":"1998"},{"key":"e_1_2_7_6_1","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.pa.20.040180.000311"},{"key":"e_1_2_7_7_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi00051a004"},{"key":"e_1_2_7_8_1","doi-asserted-by":"publisher","DOI":"10.1152\/ajpcell.1993.264.2.C361"},{"key":"e_1_2_7_9_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.280.5360.69"},{"key":"e_1_2_7_10_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi010173g"},{"key":"e_1_2_7_11_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi00251a038"},{"key":"e_1_2_7_12_1","doi-asserted-by":"publisher","DOI":"10.1016\/S1054-3589(08)60078-2"},{"key":"e_1_2_7_13_1","doi-asserted-by":"publisher","DOI":"10.1016\/0896-6273(94)90452-9"},{"key":"e_1_2_7_14_1","doi-asserted-by":"publisher","DOI":"10.1007\/s002329900084"},{"key":"e_1_2_7_15_1","doi-asserted-by":"publisher","DOI":"10.1093\/bioinformatics\/15.4.305"},{"key":"e_1_2_7_16_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1432-1033.1987.tb11173.x"},{"key":"e_1_2_7_17_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi00150a006"},{"key":"e_1_2_7_18_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi00254a015"},{"key":"e_1_2_7_19_1","first-page":"51","article-title":"MOLMOL: A program for display and analysis of macromolecular structures","volume":"14","author":"Koradi R.","year":"1996","journal-title":"structures"},{"key":"e_1_2_7_20_1","doi-asserted-by":"publisher","DOI":"10.1016\/0006-291X(80)90695-6"},{"key":"e_1_2_7_21_1","doi-asserted-by":"publisher","DOI":"10.1007\/BF00228148"},{"key":"e_1_2_7_22_1","doi-asserted-by":"publisher","DOI":"10.1016\/0006-291X(83)91093-8"},{"key":"e_1_2_7_23_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi00096a005"},{"key":"e_1_2_7_24_1","doi-asserted-by":"publisher","DOI":"10.1016\/0896-6273(95)90057-8"},{"key":"e_1_2_7_25_1","doi-asserted-by":"publisher","DOI":"10.1002\/prot.340110407"},{"key":"e_1_2_7_26_1","doi-asserted-by":"publisher","DOI":"10.1007\/BF02192855"},{"key":"e_1_2_7_27_1","doi-asserted-by":"publisher","DOI":"10.1046\/j.1432-1327.1999.00625.x"},{"key":"e_1_2_7_28_1","doi-asserted-by":"publisher","DOI":"10.1016\/0006-291X(83)91225-1"},{"key":"e_1_2_7_29_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi971044w"},{"key":"e_1_2_7_30_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0006-3495(98)77675-1"},{"key":"e_1_2_7_31_1","doi-asserted-by":"publisher","DOI":"10.1006\/abio.2000.4880"},{"key":"e_1_2_7_32_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi00168a008"},{"key":"e_1_2_7_33_1","doi-asserted-by":"publisher","DOI":"10.1093\/nar\/22.22.4673"},{"key":"e_1_2_7_34_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0165-6147(99)01398-X"},{"key":"e_1_2_7_35_1","doi-asserted-by":"publisher","DOI":"10.1016\/S1050-1738(97)00138-2"},{"key":"e_1_2_7_36_1","first-page":"953","article-title":"Noxiustoxin and leiurutoxin III, two homologous peptide toxins with binding properties to synaptosomal membrane K+ channels","volume":"27","author":"Valdivia H.H.","year":"1992","journal-title":"Biochem. 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