Articles | Volume 2, issue 2
© Author(s) 2021. This work is distributed underthe Creative Commons Attribution 4.0 License.
High-affinity tamoxifen analogues retain extensive positional disorder when bound to calmodulin
- Final revised paper (published on 13 Aug 2021)
- Supplement to the final revised paper
- Preprint (discussion started on 05 Feb 2021)
- Supplement to the preprint
Comment types: AC – author | RC – referee | CC – community | EC – editor | CEC – chief editor |
: Report abuse
RC1: 'Comment on mr-2021-7', Walter Chazin, 23 Feb 2021
- AC1: 'Reply on RC1', Jonathan Waltho, 23 Feb 2021
RC2: 'Comment on mr-2021-7', Anonymous Referee #2, 04 Mar 2021
- AC2: 'Reply on RC2', Jonathan Waltho, 19 Mar 2021
Peer review completion
AR: Author's response | RR: Referee report | ED: Editor decision
AR by Jonathan Waltho on behalf of the Authors (19 Mar 2021)  Author's response Author's tracked changes Manuscript
ED: Publish subject to minor revisions (review by editor) (22 Mar 2021) by Sebastian Hiller
AR by Jonathan Waltho on behalf of the Authors (29 Mar 2021)  Author's response Author's tracked changes Manuscript
ED: Publish as is (03 Apr 2021) by Sebastian Hiller
This manuscript presents an investigation of the interaction of calmodulin with the small molecule Tamoxifen using solution NMR. Interestingly, Tamoxifen was found to bind with high affinity without occupying specific hydrophobic pockets. This was clearly evident from the inability to satisfy inter-molecular NOEs by a single structure of the complex. The experimental approach is sound and the experiments are well designed, including several well thought out controls. This includes an important titration carried out to control for chemical shift perturbations that arise from CD3OD. The data are properly interpreted. The manuscript is well written and clear. The manuscript is suitable for publication requiring only a few typographical/grammar adjustments.
This review was performed primarily by postdoctoral fellow Randika (Randy) Perera, Ph.D.