Magnetic Resonance
Magnetic Resonance
MR
Articles | Volume 2, issue 2
Articles | Volume 2, issue 2
https://doi.org/10.5194/mr-2-629-2021
© Author(s) 2021. This work is distributed under
the Creative Commons Attribution 4.0 License.
Special issue:
https://doi.org/10.5194/mr-2-629-2021
© Author(s) 2021. This work is distributed under
the Creative Commons Attribution 4.0 License.
Articles | Volume 2, issue 2
Research article
 | 
13 Aug 2021
Research article |  | 13 Aug 2021

High-affinity tamoxifen analogues retain extensive positional disorder when bound to calmodulin

Lilia Milanesi, Clare R. Trevitt, Brian Whitehead, Andrea M. Hounslow, Salvador Tomas, Laszlo L. P. Hosszu, Christopher A. Hunter, and Jonathan P. Waltho

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Short summary
The overall aim of the study is to provide a basis from which to improve the ability of tamoxifen family drugs to reduce the activity of a secondary target protein, calmodulin, during tumour development. The main conclusion is that the binding of a tamoxifen analogue is quite unlike that of other anti-calmodulin compounds in that two drug molecules bring the two domains of calmodulin into close proximity, but they are not fixed in orientation relative to the protein.
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