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Journal Article

Structure of the mitochondrial translocator protein in complex with a diagnostic ligand.

MPS-Authors
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Jaremko,  L.
Department of NMR Based Structural Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Jaremko,  M.
Department of NMR Based Structural Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Giller,  K.
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;

/persons/resource/persons16093

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

External Resource

http://www.sciencemag.org/content/343/6177/1363.full.pdf
(Publisher version)

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Supplementary Material (public)

2008012_Suppl.pdf
(Supplementary material), 2MB

Citation

Jaremko, L., Jaremko, M., Giller, K., Becker, S., & Zweckstetter, M. (2014). Structure of the mitochondrial translocator protein in complex with a diagnostic ligand. Science, 343(6177), 1363-1366. doi:10.1126/science.1248725.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0018-F78D-4
Abstract
The 18-kilodalton translocator protein TSPO is found in mitochondrial membranes and mediates the import of cholesterol and porphyrins into mitochondria. In line with the role of TSPO in mitochondrial function, TSPO ligands are used for a variety of diagnostic and therapeutic applications in animals and humans. We present the three-dimensional high-resolution structure of mammalian TSPO reconstituted in detergent micelles in complex with its high-affinity ligand PK11195. The TSPO-PK11195 structure is described by a tight bundle of five transmembrane alpha helices that form a hydrophobic pocket accepting PK11195. Ligand-induced stabilization of the structure of TSPO suggests a molecular mechanism for the stimulation of cholesterol transport into mitochondria.