Dimerization of the pulmonary surfactant protein C in a membrane environment
Surfactant protein C (SP-C) has several functions in pulmonary surfactant. These include the transfer of lipids between different membrane structures, a role in surfactant recycling and homeostasis, and involvement in modulation of the innate defense system. Despite these important functions, the st...
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| Hauptverfasser: | , , , , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
April 27, 2022
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| In: |
PLOS ONE
Year: 2022, Jahrgang: 17, Heft: 4, Pages: 1-15 |
| ISSN: | 1932-6203 |
| DOI: | 10.1371/journal.pone.0267155 |
| Online-Zugang: | Resolving-System, kostenfrei, Volltext: https://doi.org/10.1371/journal.pone.0267155 Verlag, kostenfrei, Volltext: https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0267155 
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| Verfasserangaben: | Hanna Korolainen, Fabio Lolicato, Giray Enkavi, Jesús Pérez-Gil, Waldemar Kulig, Ilpo Vattulainen |
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| 520 | |a Surfactant protein C (SP-C) has several functions in pulmonary surfactant. These include the transfer of lipids between different membrane structures, a role in surfactant recycling and homeostasis, and involvement in modulation of the innate defense system. Despite these important functions, the structures of functional SP-C complexes have remained unclear. SP-C is known to exist as a primarily α-helical structure with an apparently unstructured N-terminal region, yet there is recent evidence that the functions of SP-C could be associated with the formation of SP-C dimers and higher oligomers. In this work, we used molecular dynamics simulations, two-dimensional umbrella sampling, and well-tempered metadynamics to study the details of SP-C dimerization. The results suggest that SP-C dimerizes in pulmonary surfactant membranes, forming dimers of different topologies. The simulations identified a dimerization motif region V21xxxVxxxGxxxM33 that is much larger than the putative A30xxxG34 motif that is commonly assumed to control the dimerization of some α-helical transmembrane domains. The results provide a stronger basis for elucidating how SP-C functions in concert with other surfactant proteins. | ||
| 650 | 4 | |a Biochemical simulations | |
| 650 | 4 | |a Dimerization | |
| 650 | 4 | |a Dimers | |
| 650 | 4 | |a Free energy | |
| 650 | 4 | |a Lipid structure | |
| 650 | 4 | |a Monomers | |
| 650 | 4 | |a Simulation and modeling | |
| 650 | 4 | |a Surfactants | |
| 700 | 1 | |a Lolicato, Fabio |e VerfasserIn |0 (DE-588)1215510608 |0 (DE-627)1726683931 |4 aut | |
| 700 | 1 | |a Enkavi, Giray |e VerfasserIn |4 aut | |
| 700 | 1 | |a Pérez-Gil, Jesús |e VerfasserIn |4 aut | |
| 700 | 1 | |a Kulig, Waldemar |e VerfasserIn |4 aut | |
| 700 | 1 | |a Vattulainen, Ilpo |e VerfasserIn |4 aut | |
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