Structure of the pore-helix of the hERG K+ channel

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dc.contributor.authorPages, Gen_AU
dc.contributor.authorTorres, AMen_AU
dc.contributor.authorJu, Pen_AU
dc.contributor.authorBansal, PSen_AU
dc.contributor.authorAlewood, PFen_AU
dc.contributor.authorKuchel, PWen_AU
dc.contributor.authorVandenberg, JIen_AU
dc.date.accessioned2010-01-21T23:42:38Zen_AU
dc.date.accessioned2010-04-30T05:05:11Zen_AU
dc.date.available2010-01-21T23:42:38Zen_AU
dc.date.available2010-04-30T05:05:11Zen_AU
dc.date.issued2009-12en_AU
dc.date.statistics2009-12en_AU
dc.description.abstractThe hERG K+ channel undergoes rapid inactivation that is mediated by 'collapse' of the selectivity filter, thereby preventing ion conduction. Previous studies have suggested that the pore-helix of hERG may be up to seven residues longer than that predicted by homology with channels with known crystal structures. In the present work, we determined structural features of a peptide from the pore loop region of hERG (residues 600-642) in both sodium dodecyl sulfate (SDS) and dodecyl phosphocholine (DPC) micelles using NMR spectroscopy. A complete structure calculation was done for the peptide in DPC, and the localization of residues inside the micelles were analysed by using a water-soluble paramagnetic reagent with both DPC and SDS micelles. The pore-helix in the hERG peptide was only two-four residues longer at the N-terminus, compared with the pore helices seen in the crystal structures of other K+ channels, rather than the seven residues suggested from previous NMR studies. The helix in the peptide spanned the same residues in both micellar environments despite a difference in the localization inside the respective micelles. To determine if the extension of the length of the helix was affected by the hydrophobic environment in the two types of micelles, we compared NMR and X-ray crystallography results from a homologous peptide from the voltage gated potassium channel, KcsA. © 2009, Springer.en_AU
dc.identifier.citationPages, G., Torres, A. M., Ju, P., Bansal, P. S., Alewood, P. F., & Kuchel, P. W., & Vandenberg, J. I. (2009). Structure of the pore-helix of the hERG K+ channel. European Biophysics Journal with Biophysics Letters, 39(1), 111-120. doi:10.1007/s00249-009-0433-1en_AU
dc.identifier.govdoc1339en_AU
dc.identifier.issn0175-7571en_AU
dc.identifier.issue1en_AU
dc.identifier.journaltitleEuropean Biophysics Journal with Biophysics Lettersen_AU
dc.identifier.pagination111-120en_AU
dc.identifier.urihttp://dx.doi.org/10.1007/s00249-009-0433-1en_AU
dc.identifier.urihttp://apo.ansto.gov.au/dspace/handle/10238/2750en_AU
dc.identifier.volume39en_AU
dc.language.isoenen_AU
dc.publisherSpringeren_AU
dc.subjectNuclear magnetic resonanceen_AU
dc.subjectCrystallographyen_AU
dc.subjectPore structureen_AU
dc.subjectPotassiumen_AU
dc.subjectPeptidesen_AU
dc.subjectSpectroscopyen_AU
dc.titleStructure of the pore-helix of the hERG K+ channelen_AU
dc.typeJournal Articleen_AU
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