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001-es BibID:BIBFORM004727
Első szerző:Hajdu Péter (biofizikus)
Cím:Drug- and mutagenesis-induced changes in the selectivity filter of a 2-pore background K+ channel / Hajdu, P., Ulens, C., Panyi, G., Tytgat, J.
Dátum:2003
Tárgyszavak:Orvostudományok Elméleti orvostudományok idézhető absztrakt
Megjelenés:Biophysical Journal. - 84 : 2 (2003), p. 93A. -
További szerzők:Ulens, Chris Panyi György (1966-) (biofizikus) Tytgat, Jan
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2.

001-es BibID:BIBFORM004726
Első szerző:Hajdu Péter (biofizikus)
Cím:Drug- and mutagenesis-induced changes in the selectivity filter of a cardiac two-pore background K+ channel / Péter Hajdú, Chris Ulens, György Panyi, Jan Tytgat
Dátum:2003
ISSN:008-6363 (Print)
Megjegyzések:As compared with voltage-gated K(+) channels (Kv-type), our knowledge of the structure-function and pharmacology of two-pore background K(+) channels is still very limited. Here we have used a drug- and mutagenesis-based approach to study the effect of the antidepressant fluoxetine (FL) and analgesic D-norpropoxyphene (NORP) on the cardiac two-pore background K(+) channel. METHODS: Whole-cell currents of the cTBAK-1 channel expressed in Xenopus laevis oocytes were investigated using conventional two-microelectrode voltage-clamp recording method combined with functional mutagenesis of the channel protein. RESULTS: Both drugs inhibit cTBAK-1 current: FL proved to be a voltage-dependent pore-blocker, while NORP induced a change in the selectivity of cTBAK-1 giving rise to a shift in the reversal potential (E(rev)) toward more positive voltages due to an increased Na(+) permeability. Mutations were introduced into the selectivity filter of the first (Y105F) and the second (F211Y) pore to mimic the P-region of HERG (GFGN) and Kv1.1 (GYGD) channels. Point mutations in the channel resulted in two distinct phenotypes of cTBAK-1: the mutant Y105F channel lost its selectivity and was unaffected by NORP, in contrast to the F211Y mutant. CONCLUSION: FL and NORP block the current of cTBAK-1 channels differently, the latter modified the selectivity of the channel pore. Our mutagenesis study revealed that NORP interacts with the selectivity filter of cTBAK-1. The significant role of the GYGD motif in this type of K(+) channels is emphasized
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Amino Acid Motifs
Analgesics
analogs and derivatives
Animals
Antidepressive Agents
Biophysics
drug effects
Female
Fluoxetine
genetics
Hungary
Ion Channels
metabolism
methods
Mice
Mutagenesis, Site-Directed
Mutation
Oocytes
pharmacology
Phenotype
Point Mutation
Potassium
Potassium Channels
Tandem Pore Domain
Propoxyphene
Research
Sodium
Support
Transcription
Xenopus laevis
Megjelenés:Cardiovascular Research. - 58 : 1 (2003), p. 46-54. -
További szerzők:Ulens, Chris Panyi György (1966-) (biofizikus) Tytgat, Jan
Internet cím:DOI
Intézményi repozitóriumban (DEA) tárolt változat
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3.

001-es BibID:BIBFORM076189
Első szerző:Krishnarjuna, Bankala
Cím:Synthesis, folding, structure and activity of a predicted peptide from the sea anemone Oulactis sp. with an ShKT fold / Krishnarjuna Bankala, Villegas-Moreno Jessica, Mitchell Michela L., Csoti Agota, Peigneur Steve, Amero Carlos, Pennington Michael W., Tytgat Jan, Panyi Gyorgy, Norton Raymond S.
Dátum:2018
ISSN:0041-0101
Megjegyzések:Sea anemone venom is rich in bioactive compounds, including peptides containing multiple disul?de bridges. In a transcriptomic study on Oulactis sp., we identi?ed the putative 36-residue peptide, OspTx2b, which is an isoform of the K channel blocker OspTx2a (Sunanda P et al. [2018] Identi?cation, chemical synthesis, structure and function of a new K V 1 channel blocking peptide from Oulactis sp. Peptide Science, in press). As OspTx2b contains a ShK/BgK-like cysteine framework, with high amino acid sequence similarity to BgK, we were interested to investigate its structure and function. The solution structure of OspTx2b was determined using nuclear magnetic resonance spectroscopy. OspTx2b does indeed possess a BgK-like sca?old, with the same disul?de bond connectivities. The orientation of the Lys-Tyr dyad in OspTx2b is more similar to that in ShK than in BgK. However, it failed to show against a range of voltage-gated potassium channels in Xenopus oocytes and human T lymphocytes. OspTx2b also showed no growth inhibitory activity against several strains of bacteria and fungi. Having a BgK-like fold with the Lys-Tyr dyad but no BgK-like activity highlights the importance of key amino acid residues in BgK that are missing in OspTx2b. The lack of activity against the KV channels assessed in this study emphasises that the ShK/BgK sca?old is capable of supporting functional activity beyond potassium channel blockade.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
OspTx2b
Cysteine-rich peptide
Sea anemone
Structure
NMR spectroscopy
Potassium channel
Megjelenés:Toxicon. - 150 (2018), p. 50-59. -
További szerzők:Villegas-Moreno, Jessica Mitchell, Michela L. Csóti Ágota (1989-) (biológus) Peigneur, Steve Amero, Carlos Pennington, Michael W. Tytgat, Jan Panyi György (1966-) (biofizikus) Norton, Raymond S.
Pályázati támogatás:Australian Research Council LP150100621
Egyéb
Australian Government Research Training Program Scholarship and a Monash University?Museum Victoria Scholarship top-up
Egyéb
CELSA/17/047 - BOF/ISP
Egyéb
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
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