Backbone and side-chain resonance assignment of the A147T polymorph of mouse TSPO in complex with a high-affinity radioligand |
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Authors: | Mariusz Jaremko Łukasz Jaremko Karin Giller Stefan Becker Markus Zweckstetter |
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Institution: | 1.Max-Planck-Institut für Biophysikalische Chemie,G?ttingen,Germany;2.Deutsches Zentrum für Neurodegenerative Erkrankungen (DZNE),G?ttingen,Germany;3.Center for Nanoscale Microscopy and Molecular Physiology of the Brain,University Medical Center,G?ttingen,Germany |
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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. |
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