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http://hdl.handle.net/2445/96367
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DC Field | Value | Language |
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dc.contributor.author | Guasch, Alicia | - |
dc.contributor.author | Aranguren Ibáñez, Álvaro | - |
dc.contributor.author | Pérez Luque, Rosa | - |
dc.contributor.author | Aparicio, David | - |
dc.contributor.author | Martínez Høyer, Sergio | - |
dc.contributor.author | Mulero Roig, María Carmen | - |
dc.contributor.author | Serrano Candelas, Eva | - |
dc.contributor.author | Pérez Riba, Mercè | - |
dc.contributor.author | Fita Rodríguez, Ignasi | - |
dc.date.accessioned | 2016-03-10T17:57:24Z | - |
dc.date.available | 2016-03-10T17:57:24Z | - |
dc.date.issued | 2015-08-06 | - |
dc.identifier.issn | 1932-6203 | - |
dc.identifier.uri | http://hdl.handle.net/2445/96367 | - |
dc.description.abstract | A limited repertoire of PPP family of serine/threonine phosphatases with a highly conserved catalytic domain acts on thousands of protein targets to orchestrate myriad central biological roles. A major structural reorganization of human calcineurin, a ubiquitous Ser/Thr PPP regulated by calcium and calmodulin and targeted by immunosuppressant drugs cyclosporin A and FK506, is unveiled here. The new conformation involves trans- to cis- isomerization of proline in the SAPNY sequence, highly conserved across PPPs, and remodels the main regulatory site where NFATc transcription factors bind. Transitions between cis- and trans- conformations may involve peptidyl prolyl isomerases such as cyclophilin A and FKBP12, which are known to physically interact with and modulate calcineurin even in the absence of immunosuppressant drugs. Alternative conformations in PPPs provide a new perspective on interactions with substrates and other protein partners and may foster development of more specific inhibitors as drug candidates. | - |
dc.format.extent | 15 p. | - |
dc.format.mimetype | application/pdf | - |
dc.language.iso | eng | - |
dc.publisher | Public Library of Science (PLoS) | - |
dc.relation.isformatof | Reproducció del document publicat a: http://dx.doi.org/10.1371/journal.pone.0134569 | - |
dc.relation.ispartof | PLoS One, 2015, vol. 10, num. 8, p. e0134569-e0134569 | - |
dc.relation.uri | http://dx.doi.org/10.1371/journal.pone.0134569 | - |
dc.rights | cc-by (c) Guasch et al., 2015 | - |
dc.rights.uri | http://creativecommons.org/licenses/by/3.0/es | - |
dc.source | Articles publicats en revistes (Biologia Cel·lular, Fisiologia i Immunologia) | - |
dc.subject.classification | Estructura cristal·lina (Sòlids) | - |
dc.subject.classification | Esterases | - |
dc.subject.classification | Síntesi de pèptids | - |
dc.subject.classification | Isomerització | - |
dc.subject.classification | Interaccions dels medicaments | - |
dc.subject.other | Layer structure (Solids) | - |
dc.subject.other | Esterases | - |
dc.subject.other | Peptide synthesis | - |
dc.subject.other | Isomerization | - |
dc.subject.other | Drug interactions | - |
dc.title | Calcineurin Undergoes a Conformational Switch Evoked via Peptidyl-Prolyl Isomerization | - |
dc.type | info:eu-repo/semantics/article | - |
dc.type | info:eu-repo/semantics/publishedVersion | - |
dc.identifier.idgrec | 657967 | - |
dc.date.updated | 2016-03-10T17:57:29Z | - |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | - |
dc.identifier.pmid | 26248042 | - |
Appears in Collections: | Articles publicats en revistes (Biologia Cel·lular, Fisiologia i Immunologia) Articles publicats en revistes (Institut d'lnvestigació Biomèdica de Bellvitge (IDIBELL)) |
Files in This Item:
File | Description | Size | Format | |
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657967.pdf | 3.78 MB | Adobe PDF | View/Open |
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