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Journal Article

Insights into cholesterol/membrane protein interactions using paramagnetic solid-state NMR.

MPS-Authors
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Giller,  K.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Leonov,  A.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Becker,  S.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Zweckstetter,  M.
Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society;

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3001351_Suppl.pdf
(Supplementary material), 794KB

Citation

Jaipuria, G., Giller, K., Leonov, A., Becker, S., & Zweckstetter, M. (2018). Insights into cholesterol/membrane protein interactions using paramagnetic solid-state NMR. Chemistry - A European Journal, 24(66), 17606-17611. doi:10.1002/chem.201804550.


Cite as: http://hdl.handle.net/21.11116/0000-0002-47D7-C
Abstract
Cholesterol is an essential component of animal cell membranes and impacts the structure and function of membrane proteins. But how cholesterol exerts its functions remains often enigmatic. Here we show that high-resolution solid-state NMR in combination with paramagnetic cholesterol analogues is a powerful approach to study the interaction of membrane proteins with cholesterol. Application of the method to the 169-residue protein TSPO provides residue-specific information about its interaction with cholesterol. Comparison with NMR signal perturbations induced by diamagnetic cholesterol furthermore supports changes in the structure of mammalian TSPO caused by cholesterol binding.