TY - JOUR
T1 - Erratum
T2 - 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)
AU - Cooper, Garry
AU - Kang, Soosung
AU - Perez-Rosello, Tamara
AU - Guzman, Jaime N.
AU - Galtieri, Daniel
AU - Xie, Zhong
AU - Kondapalli, Jyothisri
AU - Mordell, Jack
AU - Silverman, Richard B.
AU - Surmeier, D. James
N1 - Publisher Copyright:
© 2021 American Chemical Society. All rights reserved.
PY - 2021/7/16
Y1 - 2021/7/16
N2 - 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.
AB - 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.
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U2 - 10.1021/acschembio.1c00368
DO - 10.1021/acschembio.1c00368
M3 - Comment/debate
C2 - 34133142
AN - SCOPUS:85110447743
SN - 1554-8929
VL - 16
SP - 1299
EP - 1300
JO - ACS chemical biology
JF - ACS chemical biology
IS - 7
ER -