Three-dimensional structure of the actinoporin sticholysin I. Influence of long-distance effects on protein function

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dc.contributor.authorGarcía Linares, Sara
dc.contributor.authorCastrillo, Inés
dc.contributor.authorBruix, Marta
dc.contributor.authorMenéndez, Margarita
dc.contributor.authorAlegre-Cebollada, Jorge
dc.contributor.authorMartínez Del Pozo, Álvaro
dc.contributor.authorGavilanes Franco, José Gregorio
dc.date.accessioned2024-02-01T13:16:01Z
dc.date.available2024-02-01T13:16:01Z
dc.date.issued2013
dc.description.abstractActinoporins are water-soluble proteins with the ability to form pores upon insertion into biological membranes. They constitute a family of proteins with high degree of sequence identities but different hemolytic activities, suggesting that minor conformational arrangements result in major functional changes. A good example of this situation is the sea anemone Stichodactyla helianthus which produces two very similar actinoporins, sticholysins I (StnI) and II (StnII), but of very different hemolytic efficiency. Within this idea, given that the high resolution three-dimensional structure of StnII is already known, we have now solved that one corresponding to StnI in order to analyze the influence of particular residues on the conformation and activity of these proteins. In addition, random mutagenesis has been also used to produce five less hemolytic variants of StnI. All these mutations map to functionally relevant regions because they are probably involved in conformational changes associated with pore formation, which take place after membrane binding, and involve long-distance rearrangements of the polypeptide chain of actinoporins.
dc.description.departmentDepto. de Bioquímica y Biología Molecular
dc.description.facultyFac. de Ciencias Químicas
dc.description.refereedTRUE
dc.description.sponsorshipMinisterio de Ciencia e Innovación (España)
dc.description.statuspub
dc.identifier.citationGarcía-Linares, Sara, et al. «Three-Dimensional Structure of the Actinoporin Sticholysin I. Influence of Long-Distance Effects on Protein Function». Archives of Biochemistry and Biophysics, vol. 532, n.o 1, abril de 2013, pp. 39-45. https://doi.org/10.1016/j.abb.2013.01.005
dc.identifier.doi10.1016/j.abb.2013.01.005
dc.identifier.issn0003-9861
dc.identifier.officialurlhttps://doi.org/10.1016/j.abb.2013.01.005
dc.identifier.urihttps://hdl.handle.net/20.500.14352/97736
dc.journal.titleArchives of Chemistry and Biophysics
dc.language.isoeng
dc.page.final45
dc.page.initial39
dc.publisherElsevier
dc.relation.projectIDCTQ2008-00080/BQU
dc.relation.projectIDCTQ2011- 22514
dc.relation.projectIDBFU2009-10185
dc.rights.accessRightsrestricted access
dc.subject.cdu577.1
dc.subject.keywordActinoporin
dc.subject.keywordSticholysin
dc.subject.keywordNMR structure
dc.subject.keywordDynamics
dc.subject.keywordEquinatoxin
dc.subject.ucmBiología molecular (Biología)
dc.subject.unesco2406 Biofísica
dc.titleThree-dimensional structure of the actinoporin sticholysin I. Influence of long-distance effects on protein function
dc.typejournal article
dc.type.hasVersionVoR
dc.volume.number532
dspace.entity.typePublication
relation.isAuthorOfPublication35824f7f-c79d-4928-9728-21124243bf7a
relation.isAuthorOfPublication4d35a8a6-8bd3-4ff4-b179-57581d8d36d8
relation.isAuthorOfPublication4e3f8ba2-146e-4aed-9f47-f48cde58a795
relation.isAuthorOfPublication.latestForDiscovery35824f7f-c79d-4928-9728-21124243bf7a
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