Backbone and side-chain resonance assignment of the A147T polymorph of mouse TSPO in complex with a high-affinity radioligand

Mariusz Jaremko, Lukasz Jaremko, Karin Giller, Stefan Becker, Markus Zweckstetter*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

7 Scopus citations

Abstract

The integral polytopic membrane protein TSPO is the target for numerous endogenous and synthetic ligands. However, the affinity of many ligands is influenced by a common polymorphism in TSPO, in which an alanine at position 147 is replaced by threonine, thereby complicating the use of several radioligands for clinical diagnosis. In contrast, the best-characterized TSPO ligand (R)-PK11195 binds with similar affinity to both variants of mitochondrial TSPO (wild-type and A147T variant). Here we report the 1H, 13C, 15N backbone and side-chain resonance assignment of the A147T polymorph of TSPO from Mus Musculus in complex with (R)-PK11195 in DPC detergent micelles. More than 90 % of all resonances were sequence-specifically assigned, demonstrating the ability to obtain high-quality spectral data for both the backbone and the side-chains of medically relevant integral membrane proteins.

Original languageEnglish (US)
Pages (from-to)79-83
Number of pages5
JournalBiomolecular NMR Assignments
Volume10
Issue number1
DOIs
StatePublished - Apr 1 2016

Keywords

  • (R)-PK11195
  • Membrane protein
  • NMR spectroscopy
  • Polymorphism
  • TSPO

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry

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