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dc.contributor.authorOzbek, UĞUR
dc.contributor.authorWILDLING, Linda
dc.contributor.authorEBNER, Andreas
dc.contributor.authorHINTERDORFER, Peter
dc.contributor.authorCHTCHEGLOVA, Lilia A.
dc.contributor.authorAtalar, Fatmahan
dc.date.accessioned2021-03-02T22:28:44Z
dc.date.available2021-03-02T22:28:44Z
dc.date.issued2008
dc.identifier.citationCHTCHEGLOVA L. A. , Atalar F., Ozbek U., WILDLING L., EBNER A., HINTERDORFER P., "Localization of the ergtoxin-1 receptors on the voltage sensing domain of hERG K+ channel by AFM recognition imaging", PFLUGERS ARCHIV-EUROPEAN JOURNAL OF PHYSIOLOGY, cilt.456, sa.1, ss.247-254, 2008
dc.identifier.issn0031-6768
dc.identifier.othervv_1032021
dc.identifier.otherav_0ce6e0ab-3eac-4c29-8d9c-e1a30fb6865a
dc.identifier.urihttp://hdl.handle.net/20.500.12627/14283
dc.identifier.urihttps://doi.org/10.1007/s00424-007-0418-9
dc.description.abstractThe inhibition of the human ether-a-go-go-related (hERG) K+ channels is the major cause of long QT syndromes inducing fatal cardiac arrhythmias. Ergtoxin 1 (ErgTx1) belongs to scorpion-toxins, which are K+ channel-blockers, and binds to hERG channel with 1:1 stoichiometry and high affinity (K-d similar to 10 nM). Nevertheless, patch-clamp recordings recently demonstrated that ErgTx1 does not establish complete blockade of hERG currents, even at high ErgTx1 concentrations. Such phenomenon is supposed to be consistent with highly dynamic conformational changes of the outer pore domain of hERG. In this study, simultaneous topography and recognition imaging (TREC) on hERG HEK 293 cells was used to visualize binding sites on the extracellular part of hERG channel (on S1-S2 region) for Anti-K(v)11.1 (hERG-extracellular-antibody). The recognition maps of hERG channels contained recognition spots, haphazardly distributed and organized in clusters. Recognition images after the addition of ErgTx1 at high concentrations (similar to 1 mu M) revealed subsequent partial disappearance of clusters, indicating that ErgTx1 was bound to the S1-S2 region. These results were supported by AFM force spectroscopy data, showing for the first time that voltage sensing domain (S1-S4) of hERG K+ channel might be one of the multiple binding sites of ErgTx1.
dc.language.isoeng
dc.subjectYaşam Bilimleri
dc.subjectTemel Bilimler
dc.subjectSağlık Bilimleri
dc.subjectTemel Tıp Bilimleri
dc.subjectBiyokimya
dc.subjectFizyoloji
dc.subjectTıp
dc.subjectYaşam Bilimleri (LIFE)
dc.subjectBiyoloji ve Biyokimya
dc.subjectFİZYOLOJİ
dc.titleLocalization of the ergtoxin-1 receptors on the voltage sensing domain of hERG K+ channel by AFM recognition imaging
dc.typeMakale
dc.relation.journalPFLUGERS ARCHIV-EUROPEAN JOURNAL OF PHYSIOLOGY
dc.contributor.departmentJohannes Kepler University of Linz , ,
dc.identifier.volume456
dc.identifier.issue1
dc.identifier.startpage247
dc.identifier.endpage254
dc.contributor.firstauthorID59639


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