This title appears in the Scientific Report :
2020
Please use the identifier:
http://dx.doi.org/10.3390/molecules25184299 in citations.
Please use the identifier: http://hdl.handle.net/2128/25786 in citations.
Impact of Cholesterol on the Stability of Monomeric and Dimeric Forms of the Translocator Protein TSPO: A Molecular Simulation Study
Impact of Cholesterol on the Stability of Monomeric and Dimeric Forms of the Translocator Protein TSPO: A Molecular Simulation Study
The translocator protein (TSPO) is a transmembrane protein present across the three domains of life. Its functional quaternary structure consists of one or more subunits. In mice, the dimer-to-monomer equilibrium is shifted in vitro towards the monomer by adding cholesterol, a natural component of m...
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Personal Name(s): | Si Chaib, Zeineb |
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Marchetto, Alessandro / Dishnica, Klevia / Carloni, Paolo / Giorgetti, Alejandro / Rossetti, Giulia (Corresponding author) | |
Contributing Institute: |
Computational Biomedicine; IAS-5 Jülich Supercomputing Center; JSC Computational Biomedicine; INM-9 Jara-Institut Quantum Information; INM-11 |
Published in: | Molecules, 25 (2020) 18, S. 4299 - |
Imprint: |
Basel
MDPI70206
2020
|
PubMed ID: |
32961709 |
DOI: |
10.3390/molecules25184299 |
Document Type: |
Journal Article |
Research Program: |
Doktorand ohne besondere Förderung Theory, modelling and simulation Computational Science and Mathematical Methods |
Link: |
Get full text Get full text OpenAccess OpenAccess |
Publikationsportal JuSER |
Please use the identifier: http://hdl.handle.net/2128/25786 in citations.
The translocator protein (TSPO) is a transmembrane protein present across the three domains of life. Its functional quaternary structure consists of one or more subunits. In mice, the dimer-to-monomer equilibrium is shifted in vitro towards the monomer by adding cholesterol, a natural component of mammalian membranes. Here, we present a coarse-grained molecular dynamics study on the mouse protein in the presence of a physiological content and of an excess of cholesterol. The latter turns out to weaken the interfaces of the dimer by clusterizing mostly at the inter-monomeric space and pushing the contact residues apart. It also increases the compactness and the rigidity of the monomer. These two factors might play a role for the experimentally observed incremented stability of the monomeric form with increased content of cholesterol. Comparison with simulations on bacterial proteins suggests that the effect of cholesterol is much less pronounced for the latter than for the mouse protein |