Biophysical and Dynamic Characterization of Fine-Tuned Binding of the Human Respiratory Syncytial Virus M2-1 Core Domain to Long RNAs

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MetadadosDescriçãoIdioma
Autor(es): dc.contributorUniversidade Estadual Paulista (Unesp)-
Autor(es): dc.contributorUniversidade Federal do Rio de Janeiro (UFRJ)-
Autor(es): dc.contributorForchungszentrum Jülich-
Autor(es): dc.contributorHeinrich-Heine-Universität Düsseldorf-
Autor(es): dc.creatorCaruso, Icaro P. [UNESP]-
Autor(es): dc.creatorGuimarães, Giovana C. [UNESP]-
Autor(es): dc.creatorMachado, Vitor B. [UNESP]-
Autor(es): dc.creatorFossey, Marcelo A. [UNESP]-
Autor(es): dc.creatorWillbold, Dieter-
Autor(es): dc.creatorAlmeida, Fabio C.L.-
Autor(es): dc.creatorSouza, Fátima P. [UNESP]-
Data de aceite: dc.date.accessioned2022-02-22T00:48:20Z-
Data de disponibilização: dc.date.available2022-02-22T00:48:20Z-
Data de envio: dc.date.issued2021-06-25-
Data de envio: dc.date.issued2021-06-25-
Data de envio: dc.date.issued2020-11-30-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.1128/JVI.01505-20-
Fonte completa do material: dc.identifierhttp://hdl.handle.net/11449/206821-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/206821-
Descrição: dc.descriptionThe human respiratory syncytial virus (hRSV) M2-1 protein functions as a processivity and antitermination factor of the viral polymerase complex. Here, the first evidence that the hRSV M2-1 core domain (cdM2-1) alone has an unfolding activity for long RNAs is presented and the biophysical and dynamic characterization of the cdM2-1/RNA complex is provided. The main contact region of cdM2-1 with RNA was the α1-α2-α5-α6 helix bundle, which suffered local conformational changes and promoted the RNA unfolding activity. This activity may be triggered by base-pairing recognition. RNA molecules wrap around the whole cdM2-1, protruding their termini over the domain. The α2-α3 and α3-α4 loops of cdM2-1 were marked by an increase in picosecond internal motions upon RNA binding, even though they are not directly involved in the interaction. The results revealed that the cdM2-1/RNA complex originates from a fine-tuned binding, contributing to the unraveling interaction aspects necessary for M2-1 activity.-
Descrição: dc.descriptionMultiuser Center for Biomolecular Innovation (CMIB) IBILCE/UNESP-
Descrição: dc.descriptionDepartment of Physics IBILCE/UNESP-
Descrição: dc.descriptionNational Center for Nuclear Magnetic Resonance of Macromolecules Institute of Medical Biochemistry Leopoldo de Meis (IBqM) UFRJ-
Descrição: dc.descriptionNational Center for Structural Biology and Bioimaging (CENABIO) UFRJ-
Descrição: dc.descriptionInstitute of Biological Information Processing Structural Biochemistry and JuStruct (IBI-7) Forchungszentrum Jülich-
Descrição: dc.descriptionInstitut für Physikalische Biologie Heinrich-Heine-Universität Düsseldorf-
Descrição: dc.descriptionMultiuser Center for Biomolecular Innovation (CMIB) IBILCE/UNESP-
Descrição: dc.descriptionDepartment of Physics IBILCE/UNESP-
Idioma: dc.languageen-
Relação: dc.relationJournal of Virology-
???dc.source???: dc.sourceScopus-
Palavras-chave: dc.subjectFine-tuned binding-
Palavras-chave: dc.subjectHRSV M2-1 core domain-
Palavras-chave: dc.subjectMolecular docking-
Palavras-chave: dc.subjectMolecular dynamics-
Palavras-chave: dc.subjectNMR-
Palavras-chave: dc.subjectNuclear magnetic resonance-
Palavras-chave: dc.subjectRNA binding protein-
Palavras-chave: dc.subjectRNA unfolding activity-
Título: dc.titleBiophysical and Dynamic Characterization of Fine-Tuned Binding of the Human Respiratory Syncytial Virus M2-1 Core Domain to Long RNAs-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional - Unesp

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