Inhibition of the Alanine-Serine-Cysteine-1 Transporter by BMS-466442

Ivan R. Torrecillas, Susana Conde-Ceide, Ana Isabel De Lucas, Aránzazu Garcĺa Molina, Andrés A. Trabanco, Hilde Lavreysen, Leonardo Pardo, Gary Tresadern

Research output: Contribution to journalArticleResearch

1 Citation (Scopus)

Abstract

© 2019 American Chemical Society. Experiment and modeling were combined to understand inhibition of the alanine-serine-cysteine-1 (asc1) transporter. The structure-activity relationship (SAR) was explored with synthesis of analogues of BMS-466442. Direct target interaction and binding site location between TM helices 6 and 10 were confirmed via site directed mutagenesis. Computational modeling suggested the inhibitor binds via competitive occupation of the orthosteric site while also blocking the movement of TM helices that are required for transport.
Original languageEnglish
Pages (from-to)2510-2517
JournalACS Chemical Neuroscience
Volume10
DOIs
Publication statusPublished - 15 May 2019

Keywords

  • asc1
  • binding mode
  • homology model
  • mutagenesis
  • SDM
  • SLC7A10.
  • transporter

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