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Milanesi, Lilia; Trevitt, Clare R; Whitehead, Brian; Hounslow, Andrea M; Tomas, Salvador; Hosszu, Laszlo L P; Hunter, Christopher A; Waltho, Jonathan P
Magnetic Resonance : (Göttingen), 2021, Letnik: 2, Številka: 2Journal Article
Using a combination of NMR and fluorescence measurements, we have investigated the structure and dynamics of the complexes formed between calcium-loaded calmodulin (CaM) and the potent breast cancer inhibitor idoxifene, a derivative of tamoxifen. High-affinity binding ( nM) saturates with a complex. The complex is an ensemble where each idoxifene molecule is predominantly in the vicinity of one of the two hydrophobic patches of CaM but, in contrast with the lower-affinity antagonists TFP, J-8, and W-7, does not substantially occupy the hydrophobic pocket. At least four idoxifene orientations per domain of CaM are necessary to satisfy the intermolecular nuclear Overhauser effect (NOE) restraints, and this requires that the idoxifene molecules switch rapidly between positions. The CaM molecule is predominantly in the form where the N and C-terminal domains are in close proximity, allowing for the idoxifene molecules to contact both domains simultaneously. Hence, the complex illustrates how high-affinity binding occurs without the loss of extensive positional dynamics.
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