Insights into Cholesterol/Membrane Protein Interactions Using Paramagnetic Solid-State NMR
Autor: | Stefan Becker, Garima Jaipuria, Markus Zweckstetter, Karin Giller, Andrei Leonov |
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Rok vydání: | 2018 |
Předmět: |
0301 basic medicine
Catalysis DAA 1106 03 medical and health sciences chemistry.chemical_compound Mice Protein structure Receptors GABA Acetamides Translocator protein chemistry [Acetamides] Animals Amino Acid Sequence chemistry [Receptors GABA] Nuclear Magnetic Resonance Biomolecular 030102 biochemistry & molecular biology biology Bzrp protein mouse Chemistry Cholesterol chemistry [Liposomes] Phenyl Ethers Organic Chemistry Cholesterol binding chemistry [Phenyl Ethers] General Chemistry Nuclear magnetic resonance spectroscopy metabolism [Cholesterol] Protein Structure Tertiary metabolism [Receptors GABA] 030104 developmental biology Membrane Solid-state nuclear magnetic resonance Membrane protein metabolism [Acetamides] metabolism [Phenyl Ethers] ddc:540 Liposomes biology.protein Biophysics lipids (amino acids peptides and proteins) metabolism [Liposomes] chemistry [Cholesterol] Protein Binding |
Zdroj: | Chemistry-A European Journal Chemistry-a European journal 24(66), 17606-17611 (2018). doi:10.1002/chem.201804550 |
ISSN: | 1521-3765 |
DOI: | 10.1002/chem.201804550 |
Popis: | 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, high-resolution solid-state NMR in combination with paramagnetic cholesterol analogues was shown to be a powerful approach to study the interaction of membrane proteins with cholesterol. Application of the method to the 169-residue translocator 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. |
Databáze: | OpenAIRE |
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