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@ARTICLE{Combet:917018,
      author       = {Combet, Sophie and Bonneté, Françoise and Finet,
                      Stéphanie and Pozza, Alexandre and Saade, Christelle and
                      Martel, Anne and Koutsioumpas, Alexandros and Lacapère,
                      Jean-Jacques},
      title        = {{E}ffect of amphiphilic environment on the solution
                      structure of mouse {TSPO} translocator protein},
      journal      = {Biochimie},
      volume       = {205},
      issn         = {0300-9084},
      address      = {Paris [u.a.]},
      publisher    = {Elsevier},
      reportid     = {FZJ-2023-00284},
      pages        = {61-72},
      year         = {2023},
      abstract     = {The translocator protein (TSPO) is a ubiquitous
                      transmembrane protein of great pharmacological interest
                      thanks to its high affinity to many drug ligands. The only
                      high-resolution 3D-structure known for mammalian TSPO was
                      obtained by NMR for the mouse mTSPO in DPC detergent only in
                      presence of the high-affinity PK 11195 ligand. An atomic
                      structure of free-ligand mTSPO is still missing to better
                      understand the interaction of ligands with mTSPO and their
                      effects on the protein conformation.Here, we decipher the
                      solution structures of the recombinant mTSPO without ligand
                      both in (i) SDS, the detergent used to extract and purify
                      the protein from E. coli inclusion bodies, and (ii) DPC, the
                      detergent used to solve the PK 11195-binding mTSPO NMR
                      structure.We report partially refolded and less flexible
                      mTSPO helices in DPC compared to SDS. Besides, DPC
                      stabilizes the tertiary structure of mTSPO, as shown by a
                      higher intrinsic Trp fluorescence and changes in indole
                      environment.We evaluate by SEC-MALLS that ∼135 SDS and
                      ∼100 DPC molecules are bound to mTSPO. SEC-small-angle
                      X-ray (SAXS) and neutron (SANS) scattering confirm a larger
                      mTSPO-detergent complex in SDS than in DPC. Using the
                      contrast-matching technique in SEC-SANS, we demonstrate that
                      mTSPO conformation is more compact and less flexible in DPC
                      than in SDS. Combining ab initio modeling with SANS, we
                      confirm that mTSPO conformation is less elongated in DPC
                      than in SDS. However, the free-ligand mTSPO envelope in DPC
                      is not as compact as the PK 11195-binding protein NMR
                      structure, the ligand stiffening the protein.},
      cin          = {JCNS-FRM-II / MLZ / JCNS-1 / JCNS-4},
      ddc          = {540},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 / I:(DE-588b)4597118-3 /
                      I:(DE-Juel1)JCNS-1-20110106 / I:(DE-Juel1)JCNS-4-20201012},
      pnm          = {6G4 - Jülich Centre for Neutron Research (JCNS) (FZJ)
                      (POF4-6G4) / 632 - Materials – Quantum, Complex and
                      Functional Materials (POF4-632)},
      pid          = {G:(DE-HGF)POF4-6G4 / G:(DE-HGF)POF4-632},
      experiment   = {EXP:(DE-MLZ)NOSPEC-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {36460205},
      UT           = {WOS:000943144700001},
      doi          = {10.1016/j.biochi.2022.11.014},
      url          = {https://juser.fz-juelich.de/record/917018},
}