Journal
BIOMOLECULAR NMR ASSIGNMENTS
Volume 10, Issue 1, Pages 79-83Publisher
SPRINGER
DOI: 10.1007/s12104-015-9642-y
Keywords
TSPO; Polymorphism; (R)-PK11195; NMR spectroscopy; Membrane protein
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Funding
- DFG Collaborative Research Center 803
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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 H-1, C-13, N-15 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.
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