Structure of the mammalian TSPO/PBR protein

Mariusz Jaremko, Lukasz Jaremko, Garima Jaipuria, Stefan Becker, Markus Zweckstetter*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

19 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)566-571
Number of pages6
JournalBiochemical Society Transactions
Volume43
DOIs
StatePublished - Aug 1 2015

Keywords

  • 1-(2-chlorophenyl)-N-methyl-N-(1-methylpropyl)-3-isoquinolinecarboxamide (PK11195)
  • Dynamics
  • Nuclear magnetic resonance (NMR)
  • Peripheral benzodiazepine receptor
  • Structure
  • TSPO

ASJC Scopus subject areas

  • Biochemistry

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