Erratum: A single amino acid determines the selectivity and efficacy of selective negative allosteric modulators of CaV1.3 L-type calcium channels (ACS Chemical Biology (2020) 15:9 (2539-2550)DOI: 10.1021/acschembio.0c00577)

Garry Cooper, Soosung Kang, Tamara Perez-Rosello, Jaime N. Guzman, Daniel Galtieri, Zhong Xie, Jyothisri Kondapalli, Jack Mordell, Richard B. Silverman*, D. James Surmeier

*Corresponding author for this work

Research output: Contribution to journalComment/debatepeer-review

Abstract

In the Introduction, the following should be changed: From these studies, it was realized that the previously reported study that failed to see cp-PYT inhibition14 used a variant of the CaV1.3 subunit lacking this key single amino acid residue, thereby abolishing the activity of cp-PYT. The corrected passage is as follows: From these studies, it was realized that the previously reported study that failed to see cp- PYT inhibition14 used a splice variant of the CaV1.3 subunit containing exon 31A instead of exon 31; computational homology modeling suggests that this splice variant alters the conformation of the DHP binding pocket, thereby lowering the cp-PYT af f inity. In the Discussion, the following should be changed: The cloned α1 subunit used in their experiments, however, had a mutation at methionine 1078, the residue in native channels now shown to be critical for the binding of cp-PYT to the DHP site (Figure 2). The corrected passage is as follows: The cloned α1 subunit used in their experiments was alternatively spliced to contain exon 31A instead of exon 31; computational homology modeling suggests that this splice variant alters the conformation of the DHP binding pocket, thereby lowering the cp-PYT af f inity.

Original languageEnglish (US)
Pages (from-to)1299-1300
Number of pages2
JournalACS chemical biology
Volume16
Issue number7
DOIs
StatePublished - Jul 16 2021

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine

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