{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T04:41:37Z","timestamp":1791348097477,"version":"4.3.1"},"reference-count":49,"publisher":"Wiley","issue":"3","license":[{"start":{"date-parts":[[2004,4,27]],"date-time":"2004-04-27T00:00:00Z","timestamp":1083024000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["J of Molecular Recognition"],"published-print":{"date-parts":[[2004,5]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>ERG potassium channels specify one component of the delayed rectifier in the heart and are likely to play an important functional role in other excitable cells. Compared to other K<jats:sup>+<\/jats:sup> channels, the human ERG (hERG) channel possesses an unusually long S5\u2010P linker that presumably forms an alpha\u2010helix important for channel function. hERG\u2010specific toxins bind to the outer mouth of the hERG channel. Channel residues in the middle of the S5\u2010P linker and at the pore entrance are critical for toxin binding. One of these scorpion toxins is BeKm\u20101. Residues critical for BeKm\u20101 binding to the hERG channel are located in the alpha\u2010helix and the following loop, whereas the \u2018traditional\u2019 interaction surface of other short scorpion toxins is formed by residues on the \u03b2\u2010sheet. This unique localization of BeKm\u20101's interaction surface and its specific action on the hERG channel suggest a unique outer mouth structure of the hERG channel. We used the mutant cycle analysis approach to define contacts in the toxin\u2013channel complex. This information provides critical constraints and is important for molecular modeling of the hERG pore structure. Copyright \u00a9 2004 John Wiley &amp; Sons, Ltd.<\/jats:p>","DOI":"10.1002\/jmr.667","type":"journal-article","created":{"date-parts":[[2004,4,27]],"date-time":"2004-04-27T12:03:21Z","timestamp":1083067401000},"page":"209-217","source":"Crossref","is-referenced-by-count":29,"title":["Unique interaction of scorpion toxins with the hERG channel"],"prefix":"10.1002","volume":"17","author":[{"given":"Yuliya V.","family":"Korolkova","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gea\u2010Ny","family":"Tseng","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Eugene V.","family":"Grishin","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2004,4,27]]},"reference":[{"key":"e_1_2_1_2_1","doi-asserted-by":"publisher","DOI":"10.1016\/0896-6273(95)90104-3"},{"key":"e_1_2_1_3_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.271.49.31013"},{"key":"e_1_2_1_4_1","doi-asserted-by":"publisher","DOI":"10.1016\/S1570-9639(02)00458-2"},{"key":"e_1_2_1_5_1","doi-asserted-by":"publisher","DOI":"10.1038\/283673a0"},{"key":"e_1_2_1_6_1","first-page":"131","volume-title":"Perspectives in Drug Discovery and Design 15\/6","author":"Castle N","year":"1999"},{"key":"e_1_2_1_7_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi9724927"},{"key":"e_1_2_1_8_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1749-6632.1999.tb11293.x"},{"key":"e_1_2_1_9_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0014-5793(02)03652-9"},{"key":"e_1_2_1_10_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0022-2836(02)00095-5"},{"key":"e_1_2_1_11_1","doi-asserted-by":"publisher","DOI":"10.1124\/mol.64.1.59"},{"key":"e_1_2_1_12_1","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1007\/s004249900101","article-title":"Allosteric effects of mutations in the extracellular S5\u2010P loop on the gating and ion permeation properties of the hERG potassium channel","volume":"439","author":"Dun W","year":"1999","journal-title":"Pflugers Arch."},{"key":"e_1_2_1_13_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0006-3495(99)77464-3"},{"key":"e_1_2_1_14_1","doi-asserted-by":"publisher","DOI":"10.1016\/0014-5793(96)00333-X"},{"key":"e_1_2_1_15_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0076-6879(99)94035-1"},{"key":"e_1_2_1_16_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0041-0101(00)00214-2"},{"key":"e_1_2_1_17_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0896-6273(00)80057-4"},{"key":"e_1_2_1_18_1","doi-asserted-by":"publisher","DOI":"10.1096\/fasebj.13.8.953"},{"key":"e_1_2_1_19_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.7716527"},{"key":"e_1_2_1_20_1","article-title":"BmTx3, a scorpion toxin with two putative functional faces separately active on A\u2010type K+ and HERG currents","author":"Huys I","year":"2003","journal-title":"Biochem. 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