Dimerization of the pulmonary surfactant protein C in a membrane environment

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dc.contributor.authorKorolainen, Hanna
dc.contributor.authorLolicato, Fabio
dc.contributor.authorEnkavi, Giray
dc.contributor.authorPérez Gil, Jesús
dc.contributor.authorKulig, Waldemar
dc.contributor.authorVattulainen, Ilpo
dc.date.accessioned2023-06-22T10:53:48Z
dc.date.available2023-06-22T10:53:48Z
dc.date.issued2022-04-27
dc.description.abstractSurfactant 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.
dc.description.departmentSección Deptal. de Bioquímica y Biología Molecular (Biológicas)
dc.description.facultyFac. de Ciencias Biológicas
dc.description.refereedTRUE
dc.description.sponsorshipMinisterio de Ciencia e Innovación (MICINN)
dc.description.sponsorshipComunidad de Madrid
dc.description.sponsorshipAcademy of Finland
dc.description.sponsorshipDoctoral Programme in Materials Research and Nanosciences (MATRENA)
dc.description.statuspub
dc.eprint.idhttps://eprints.ucm.es/id/eprint/74033
dc.identifier.doi10.1371/journal.pone.0267155
dc.identifier.issn1932-6203
dc.identifier.officialurlhttps://doi.org/10.1371/journal.pone.0267155
dc.identifier.relatedurlhttps://journals.plos.org/plosone/article?id=10.1371/journal.pone.0267155
dc.identifier.urihttps://hdl.handle.net/20.500.14352/71853
dc.issue.number4
dc.journal.titlePLoS ONE
dc.language.isoeng
dc.page.final15
dc.page.initial1
dc.publisherPublic Library Science
dc.relation.projectID(RTI2018-094564-B-100)
dc.relation.projectID(P2018/NMT-4389)
dc.relation.projectID(grant no. 307415)
dc.rightsAtribución 3.0 España
dc.rights.accessRightsopen access
dc.rights.urihttps://creativecommons.org/licenses/by/3.0/es/
dc.subject.cdu577.112
dc.subject.keywordPulmonary surfactant protein C
dc.subject.keywordDimerization
dc.subject.ucmBioquímica (Biología)
dc.subject.unesco2302 Bioquímica
dc.titleDimerization of the pulmonary surfactant protein C in a membrane environment
dc.typejournal article
dc.volume.number17
dspace.entity.typePublication
relation.isAuthorOfPublicationbcddc7b1-6137-48ba-921d-4abd534dfd49
relation.isAuthorOfPublication.latestForDiscoverybcddc7b1-6137-48ba-921d-4abd534dfd49
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