Insights into Cholesterol/Membrane Protein Interactions Using Paramagnetic Solid-State NMR

Autor: Stefan Becker, Garima Jaipuria, Markus Zweckstetter, Karin Giller, Andrei Leonov
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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