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Journal Article

Structure of the mammalian TSPO/PBR protein.

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

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Jaremko,  L.
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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http://www.biochemsoctrans.org/content/43/4/566.full-text.pdf
(Publisher version)

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Fulltext (public)

2182120.pdf
(Publisher version), 476KB

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Citation

Jaremko, M., Jaremko, L., Jaipuria, G., Becker, S., & Zweckstetter, M. (2015). Structure of the mammalian TSPO/PBR protein. Biochemical Society Transactions, 43(4), 566-571. doi:10.1042/BST20150029.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0028-3A09-D
Abstract
The 3D structure of the 18-kDa transmembrane (TM) protein TSPO (translocator protein)/PBR (peripheral benzodiazepine receptor), which contains a binding site for benzodiazepines, is important to better understand its function and regulation by endogenous and synthetic ligands. We have recently determined the structure of mammalian TSPO/PBR in complex with the diagnostic ligand PK11195 [1-(2-chlorophenyl)-N-methyl-N-(1-methylpropyl)-3-isoquinolinecarboxamide; Jaremko et al. (2014) Science 343, 1363-1366], providing for the first time atomic-level insight into the conformation of this protein, which is up-regulated in various pathological conditions including Alzheimer's disease and Parkinson's disease. Here, we review the studies which have probed the structural properties of mammalian TSPO/PBR as well as the homologues bacterial tryptophan-rich sensory proteins (TspOs) over the years and provide detailed insight into the 3D structure of mouse TSPO (mTSPO)/PBR in complex with PK11195.