{"refrec":{"BRefID":127371,"RR":"<b>Fan, C.X.; Chen, X.K.; Zhang, C.; Wang, L.X.; Duan, K.L.; He, L.L.; Cao, Y.; Liu, S.Y.; Zhong, M.N.; Ulens, C.; Tytgat, J.; Chen, J.S.; Chi, C.W.; Zhou, Z.</b> (2003). A novel conotoxin from <i>Conus betulinus</i>, kappa-BtX, unique in cysteine pattern and in function as a specific BK channel modulator. <i>J. Biol. Chem. 278(15)</i>: 12624-12633. <a href=\"https://dx.doi.org/10.1074/jbc.M210200200\" target=\"_blank\">https://dx.doi.org/10.1074/jbc.M210200200</a>","BEntID":121440,"PublicFlag":1,"CheckedFlag":0,"wosflag":1,"vabbflag":1,"RefStringPartII":". <i>J. Biol. Chem. 278(15)</i>: 12624-12633. <a href=\"https://dx.doi.org/10.1074/jbc.M210200200\" target=\"_blank\">https://dx.doi.org/10.1074/jbc.M210200200</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":1,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Fan, C.X.; Chen, X.K.; Zhang, C.; Wang, L.X.; Duan, K.L.; He, L.L.; Cao, Y.; Liu, S.Y.; Zhong, M.N.; Ulens, C.; Tytgat, J.; Chen, J.S.; Chi, C.W.; Zhou, Z.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Fan, C.X. <i>et al.</i>","Englishabstract":"A novel conotoxin, kappa-conotoxin (kappa-BtX), has been purified and characterized from the venom of a worm-hunting cone snail, <i>Conus betulinus</i>. The toxin, with four disulfide bonds, shares no sequence homology with any other conotoxins. Based on a partial amino acid sequence, its cDNA was cloned and sequenced. The deduced sequence consists of a 26-residue putative signal peptide, a 31-residue mature toxin, and a 13-residue extra peptide at the C terminus. The extra peptide is cleaved off by proteinase post-processing. All three Glu residues are gamma-carboxylated, one of the two Pro residues is hydroxylated at position 27, and its C-terminal residue is Pro-amidated. The monoisotopic mass of the toxin is 3569.0 Da. Electrophysiological experiments show that: 1) among voltage-gated channels;, K-BtX is a specific modulator of K+ channels; 2) among the K channels, kappa-BtX specifically up-modulates the Ca2+- and voltage-sensitive BK channels (252 47%); 3) its EC50 is 0.7 nm with a single binding site (Hill = 0.88); 4) the time constant of wash-out is 8.3 s; and 5) kappa-BtX has no effect on single channel conductance, but increases the open probability of BK channels. It is concluded that kappa-BtX is a novel specific biotoxin against BK channels.","AbstractOtherLang":null,"BibLvlCode":"AS","StandardTitle":"A novel conotoxin from <i>Conus betulinus</i>, kappa-BtX, unique in cysteine pattern and in function as a specific BK channel modulator","OrigTitleLangCode":"en","OrigTitleLangCodeExtended":"eng","OrigTitleLangID":15,"DateLastModified":{"date":"2026-04-17 01:31:43.067358","timezone_type":1,"timezone":"+02:00"},"UserAccessRight":null,"UserAccID":null,"AuthorKeywords":null,"OtherDescriptors":null,"Notes":null,"AnaPub":2003,"MonPub":null,"DateUpdate":"2012-12-07","DateCreate":"2008-11-04","SecASFANote":null,"ConfID":null,"PeerRev":1,"VlizCoreFlag":1,"WoScode":"WOS:000182189500007","VABBcode":null,"OpenAcc":0,"DOI":"10.1074/jbc.M210200200"},"refs":null,"anarec":{"AnaID":127371,"PubliDate":2003,"Pagination":"12624-12633","XtraPublOfAnaID":null,"ISBN":null,"Volume":"278","Issue":"15","BRefMon":null,"BRefMonRR":null,"BRefXtra":null,"BRefXtraRR":null,"SerBRefID":43206,"SerRR":"Journal of Biological Chemistry. 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