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 language | English |
|---|---|
| Pages (from-to) | 1299-1300 |
| Number of pages | 2 |
| Journal | ACS Chemical Biology |
| Volume | 16 |
| Issue number | 7 |
| DOIs |
|
| State | Published - 16 Jul 2021 |
Bibliographical note
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Dive into the research topics of '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)'. Together they form a unique fingerprint.Cite this
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