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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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Main Authors: Korolainen, Hanna (Author) , Lolicato, Fabio (Author) , Enkavi, Giray (Author) , Pérez-Gil, Jesús (Author) , Kulig, Waldemar (Author) , Vattulainen, Ilpo (Author)
Format: Article (Journal)
Language:English
Published: April 27, 2022
In: PLOS ONE
Year: 2022, Volume: 17, Issue: 4, Pages: 1-15
ISSN:1932-6203
DOI:10.1371/journal.pone.0267155
Online Access: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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Author Notes:Hanna Korolainen, Fabio Lolicato, Giray Enkavi, Jesús Pérez-Gil, Waldemar Kulig, Ilpo Vattulainen
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Summary: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.
Item Description:Gesehen am 22.11.2022
Physical Description:Online Resource
ISSN:1932-6203
DOI:10.1371/journal.pone.0267155

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