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Dimerization of the pulmonary surfactant protein C in a membrane environment



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Korolainen, Hanna and Lolicato, Fabio and Enkavi, Giray and Pérez Gil, Jesús and Kulig, Waldemar and Vattulainen, Ilpo (2022) Dimerization of the pulmonary surfactant protein C in a membrane environment. PLoS ONE, 17 (4). pp. 1-15. ISSN 1932-6203

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Official URL: https://doi.org/10.1371/journal.pone.0267155


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 Type:Article
Uncontrolled Keywords:Pulmonary surfactant protein C; Dimerization
Subjects:Medical sciences > Biology > Biochemistry
ID Code:74033
Deposited On:29 Jul 2022 09:06
Last Modified:03 Aug 2022 11:16

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