ArticleInternational journal of molecular sciences2018
Structural Prediction of the Dimeric Form of the Mammalian Translocator Membrane Protein TSPO: A Key Target for Brain Diagnostics.
Article in International journal of molecular sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 18 citations in OpenAlex.
- TSPO protein binding partners in bacteria, animals, and plants.Journal of bioenergetics and biomembranes · 2021Review
- The Interplay of Cholesterol and Ligand Binding inMolecules (Basel, Switzerland) · 2021Article
- Membrane-Mediated Ligand Unbinding of the PK-11195 Ligand from TSPO.Biophysical journal · 2021Article
- Impact of Cholesterol on the Stability of Monomeric and Dimeric Forms of the Translocator Protein TSPO: A Molecular Simulation Study.Molecules (Basel, Switzerland) · 2020Article
- Insight into the Structural Features of TSPO: Implications for Drug Development.Trends in pharmacological sciences · 2020Review
- Applications of water molecules for analysis of macromolecule properties.Computational and structural biotechnology journal · 2020Review
- Characterization of the High-Affinity Drug Ligand Binding Site of Mouse Recombinant TSPO.International journal of molecular sciences · 2019Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 3 countries.
Funding
Abstract
Positron emission tomography (PET) radioligands targeting the human translocator membrane protein (TSPO) are broadly used for the investigations of neuroinflammatory conditions associated with neurological disorders. Structural information on the mammalian protein homodimers-the suggested functional state of the protein-is limited to a solid-state nuclear magnetic resonance (NMR) study and to a model based on the previously-deposited solution NMR structure of the monomeric mouse protein. Computational studies performed here suggest that the NMR-solved structure in the presence of detergents is not prone to dimer formation and is furthermore unstable in its native membrane environment. We, therefore, propose a new model of the functionally-relevant dimeric form of the mouse protein, based on a prokaryotic homologue. The model, fully consistent with solid-state NMR data, is very different from the previous predictions. Hence, it provides, for the first time, structural insights into this pharmaceutically-important target which are fully consistent with experimental data.
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Registered trials
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