Journal
PLOS ONE
Volume 17, Issue 4, Pages -Publisher
PUBLIC LIBRARY SCIENCE
DOI: 10.1371/journal.pone.0267155
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Funding
- Academy of Finland [307415]
- Doctoral Programme in Materials Research and Nanosciences (MATRENA)
- Spanish Ministry of Science and Innovation [RTI2018-094564-B-100]
- regional Government of Madrid [P2018/NMT-4389]
- CSC-IT Centre for Science Ltd. (Espoo, Finland)
- Finnish Grid and Cloud Infrastructure [urn:nbn:fi:research-infras-2016072533]
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This study investigated the details of SP-C dimerization using molecular dynamics simulations. The results revealed that SP-C dimerizes in pulmonary surfactant membranes and forms dimers with different topologies. These findings provide a stronger basis for understanding how SP-C functions together with other surfactant proteins.
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 alpha-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 V(21)xxxVxxxGxxxM(33) that is much larger than the putative A(30)xxxG(34) motif that is commonly assumed to control the dimerization of some alpha-helical transmembrane domains. The results provide a stronger basis for elucidating how SP-C functions in concert with other surfactant proteins.
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