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dc.contributor.authorBorges, Rafael J. [UNESP]
dc.contributor.authorLemke, Ney [UNESP]
dc.contributor.authorFontes, Marcos R. M. [UNESP]
dc.date.accessioned2018-12-11T17:34:53Z
dc.date.available2018-12-11T17:34:53Z
dc.date.issued2017-12-01
dc.identifierhttp://dx.doi.org/10.1038/s41598-017-15614-z
dc.identifier.citationScientific Reports, v. 7, n. 1, 2017.
dc.identifier.issn2045-2322
dc.identifier.urihttp://hdl.handle.net/11449/179365
dc.description.abstractPhospholipase A2-like (PLA2-like) proteins contribute to the development of muscle necrosis in Viperidae snake bites and are not efficiently neutralized by current antivenom treatments. The toxic mechanisms of PLA2-like proteins are devoid of catalytic activity and not yet fully understood, although structural and functional experiments suggest a dimeric assembly and that the C-terminal residues are essential to myotoxicity. Herein, we characterized the functional mechanism of bothropic PLA2-like structures related to global and local measurements using the available models in the Protein Data Bank and normal mode molecular dynamics (NM-MD). Those measurements include: (i) new geometric descriptions between their monomers, based on Euler angles; (ii) characterizations of canonical and non-canonical conformations of the C-terminal residues; (iii) accessibility of the hydrophobic channel; (iv) inspection of ligands; and (v) distance of clustered residues to toxin interface of interaction. Thus, we described the allosteric activation of PLA2-like proteins and hypothesized that the natural movement between monomers, calculated from NM-MD, is related to their membrane disruption mechanism, which is important for future studies of the inhibition process. These methods and strategies can be applied to other proteins to help understand their mechanisms of action.en
dc.language.isoeng
dc.relation.ispartofScientific Reports
dc.sourceScopus
dc.titlePLA2-like proteins myotoxic mechanism: A dynamic model descriptionen
dc.typeArtigo
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)
dc.description.affiliationDepartamento de Física e Biofísica Instituto de Biociências Universidade Estadual Paulista (UNESP)
dc.description.affiliationUnespDepartamento de Física e Biofísica Instituto de Biociências Universidade Estadual Paulista (UNESP)
dc.identifier.doi10.1038/s41598-017-15614-z
dc.rights.accessRightsAcesso aberto
dc.identifier.scopus2-s2.0-85034106030
dc.identifier.file2-s2.0-85034106030.pdf
dc.relation.ispartofsjr1,533
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