Elucidating the clandestine behavior of enantiomeric DHPs in calcium channels
Author:
Affiliation:
1. Leibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP) 1 , Berlin, Germany
2. Institute of Chemistry, Technical University of Berlin 2 , Berlin, Germany
Abstract
Funder
Leibniz-Forschungsinstitut für Molekulare Pharmakologie
Publisher
Rockefeller University Press
Subject
Physiology
Link
https://rupress.org/jgp/article-pdf/doi/10.1085/jgp.202313481/1919426/jgp_202313481.pdf
Reference10 articles.
1. Modulation of pore opening of eukaryotic sodium channels by π-helices in S6;Choudhury;J. Phys. Chem. Lett.,2023
2. An open state of a voltage-gated sodium channel involving a π-helix and conserved pore-facing asparagine;Choudhury;Biophys. J.,2022
3. Evolutionary origin of a secondary structure: π-Helices as cryptic but widespread insertional variations of α-helices that enhance protein functionality;Cooley;J. Mol. Biol.,2010
4. Structural basis of the modulation of the voltage-gated calcium ion channel Cav 1.1 by dihydropyridine compounds;Gao;Angew. Chem. Int. Ed. Engl,2021
5. L-type calcium channels: The low down;Lipscombe;J. Neurophysiol,2004
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