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

Jaremko, M., Jaremko, L., Giller, K., Becker, S., & Zweckstetter, M. (2016). Backbone and side-chain resonance assignment of the A147T polymorph of mouse TSPO in complex with a high-affinity radioligand. Biomolecular NMR Assignments, 10(1), 79-83. doi:10.1007/s12104-015-9642-y.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-2222-3 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-C575-2
Genre: Journal Article

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2262636.pdf (Publisher version), 2MB
 
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 Creators:
Jaremko, M.1, Author              
Jaremko, L.1, Author              
Giller, K.2, Author              
Becker, S.2, Author              
Zweckstetter, M.1, Author              
Affiliations:
1Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society, ou_578571              
2Department of NMR-Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              

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Free keywords: TSPO; Polymorphism; (R)-PK11195; NMR spectroscopy; Membrane protein
 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 (1)H, (13)C, (15)N 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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Language(s): eng - English
 Dates: 2015-09-122016-04
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1007/s12104-015-9642-y
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Title: Biomolecular NMR Assignments
Source Genre: Journal
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Pages: - Volume / Issue: 10 (1) Sequence Number: - Start / End Page: 79 - 83 Identifier: -