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  Toward the functional oligomerization state of tryptophan-rich sensory proteins.

Jaremko, L., Jaremko, M., Becker, S., & Zweckstetter, M. (2014). Toward the functional oligomerization state of tryptophan-rich sensory proteins. Protein Science, 23(8), 1154-1160. doi:10.1002/pro.2487.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-001A-0C19-0 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-616F-6
Genre: Journal Article

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 Creators:
Jaremko, L.1, Author              
Jaremko, M.1, Author              
Becker, S.1, Author              
Zweckstetter, M.2, Author              
Affiliations:
1Department of NMR Based Structural Biology, MPI for Biophysical Chemistry, Max Planck Society, ou_578567              
2Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society, ou_578571              

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Free keywords: mitochondria; membrane protein; receptor; structure; oligomerization
 Abstract: A conserved family of tryptophan-rich sensory proteins (TspO) mediates the transport of heme degradation intermediates across membranes. In eukaryotes, the homologous mitochondrial translocator protein (TSPO) binds cholesterol and radioligands as monomer. On the basis of the mammalian TSPO structure, bioinformatic analysis, and a 10 Å resolution electron microscopy map of TspO from Rhodobacter sphaeroides, we developed a model of the tertiary and quaternary structure of TspO that is in agreement with available mutagenesis data. Our study provides insight into the conformational basis for the restricted interaction of bacterial TspO with radioligands and the functional oligomerization state of bacterial TspO proteins.

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Language(s): eng - English
 Dates: 2014-05-102014-08
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1002/pro.2487
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Title: Protein Science
Source Genre: Journal
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Pages: - Volume / Issue: 23 (8) Sequence Number: - Start / End Page: 1154 - 1160 Identifier: -