Crystal structures of BnSP-7 and BnSP-6, two Lys49-phospholipases A(2): quaternary structure and inhibition mechanism insights

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dc.contributor.authorMagro, A. J.
dc.contributor.authorSoares, A. M.
dc.contributor.authorGiglio, JR
dc.contributor.authorFontes, MRM
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionUNAERP
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.date.accessioned2014-05-20T13:49:23Z
dc.date.available2014-05-20T13:49:23Z
dc.date.issued2003-11-21
dc.description.abstractPhospholipases A(2) are components of Bothrops venoms responsible for disruption of cell membrane integrity via hydrolysis of its phospholipids. A class of PLA(2)-like proteins has been described which despite PLA(2) activity on artificial substrate, due to a D49K mutation, is still highly myonecrotic. This work reports the X-ray structure determination of two Lys49-PLA(2)s from Bothrops neuwiedi pauloensis (BnSP-7 and BnSP-6) and, for the first time, the comparison of eight dimeric Lys49-PLA2s. This comparison reveals that there are not just two (open and closed) but at least six different conformations. The binding of fatty acid observed in three recent Lys49-PLA(2) structures seems to be independent of their quaternary conformation. Cys29 polarization by Lys122 is not significant for BnSP-7 and BnSP-6 or other structures not bound by fatty acids. These structures may be in an active state when nothing is bound to them and the Lys122/Cys29 interactions are weak or absent. (C) 2003 Elsevier B.V. All rights reserved.en
dc.description.affiliationUniv Estadual Paulista Julio Mesquita Filho, Dept Fis & Biofis, IB, Botucatu, SP, Brazil
dc.description.affiliationUNAERP, Dept Biotechnol, Ribeirao Preto, SP, Brazil
dc.description.affiliationUSP, FMRP, Dept Bioquim & Imunol, Ribeirao Preto, SP, Brazil
dc.description.affiliationUnespUniv Estadual Paulista Julio Mesquita Filho, Dept Fis & Biofis, IB, Botucatu, SP, Brazil
dc.format.extent713-720
dc.identifierhttp://dx.doi.org/10.1016/j.bbrc.2003.10.047
dc.identifier.citationBiochemical and Biophysical Research Communications. San Diego: Academic Press Inc. Elsevier B.V., v. 311, n. 3, p. 713-720, 2003.
dc.identifier.doi10.1016/j.bbrc.2003.10.047
dc.identifier.issn0006-291X
dc.identifier.urihttp://hdl.handle.net/11449/17603
dc.identifier.wosWOS:000186643100026
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofBiochemical and Biophysical Research Communications
dc.relation.ispartofjcr2.559
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.subjectphospholipase A(2)pt
dc.subjectmyotoxinpt
dc.subjectcrystal structurept
dc.subjectbothropic venompt
dc.subjectquaternary structure changespt
dc.subjectlack of catalytic mechanismpt
dc.titleCrystal structures of BnSP-7 and BnSP-6, two Lys49-phospholipases A(2): quaternary structure and inhibition mechanism insightsen
dc.typeArtigo
dcterms.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dcterms.rightsHolderElsevier B.V.
unesp.author.lattes0059017255172730[1]
unesp.author.orcid0000-0002-4634-6221[4]
unesp.author.orcid0000-0002-4253-6992[1]
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Biociências, Botucatupt

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Artigos - Física e Biofísica - IBB