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  Conformational flexibility in the transmembrane protein TSPO.

Jaremko, L., Jaremko, M., Giller, K., Becker, S., & Zweckstetter, M. (2015). Conformational flexibility in the transmembrane protein TSPO. Chemistry-A European Journal, 21(46), 16555-16563. doi:10.1002/chem.201502314.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-29BA-6 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-BD05-2
Genre: Journal Article

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 Creators:
Jaremko, L.1, Author              
Jaremko, M.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: NMR spectroscopy; dynamics; function; membrane proteins; small molecules; structure
 Abstract: The translocator protein (TSPO) is an integral membrane protein that interacts with a wide variety of endogenous ligands, such as cholesterol and porphyrins, and is also the target for several small molecules with substantial in vivo efficacy. When complexed with the TSPO-specific radioligand (R)-PK11195, TSPO folds into a rigid five-helix bundle. However, little is known about the structure and dynamics of TSPO in the absence of high-affinity ligands. By means of NMR spectroscopy, we show that TSPO exchanges between multiple conformations in the absence of (R)-PK11195. Extensive motions on time scales from pico- to microseconds occur all along the primary sequence of the protein, leading to a loss of stable tertiary interactions and local unfolding of the helical structure in the vicinity of the ligand-binding site. The flexible nature of TSPO highlights the importance of conformational plasticity in integral membrane proteins.

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Language(s): eng - English
 Dates: 2015-09-232015-11-09
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1002/chem.201502314
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Title: Chemistry-A European Journal
Source Genre: Journal
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Pages: - Volume / Issue: 21 (46) Sequence Number: - Start / End Page: 16555 - 16563 Identifier: -