Deutsch
 
Benutzerhandbuch Datenschutzhinweis Impressum Kontakt
  DetailsucheBrowse

Datensatz

DATENSATZ AKTIONENEXPORT

Freigegeben

Zeitschriftenartikel

Conformational flexibility in the transmembrane protein TSPO.

MPG-Autoren
/persons/resource/persons84653

Jaremko,  L.
Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons84648

Jaremko,  M.
Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons36496

Giller,  K.
Department of NMR Based Structural Biology, MPI for Biophysical Chemistry, Max Planck Society;

/persons/resource/persons14824

Becker,  S.
Department of NMR Based Structural Biology, MPI for Biophysical Chemistry, Max Planck Society;

/persons/resource/persons16093

Zweckstetter,  M.
Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society;

Volltexte (frei zugänglich)
Es sind keine frei zugänglichen Volltexte verfügbar
Ergänzendes Material (frei zugänglich)

2179738_Suppl.pdf
(Ergänzendes Material), 898KB

Zitation

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.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0028-29BA-6
Zusammenfassung
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.