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dc.contributor.authorMagro, A. J.-
dc.contributor.authorSoares, A. M.-
dc.contributor.authorGiglio, JR-
dc.contributor.authorFontes, MRM-
dc.identifier.citationBiochemical and Biophysical Research Communications. San Diego: Academic Press Inc. Elsevier B.V., v. 311, n. 3, p. 713-720, 2003.-
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.publisherElsevier B.V.-
dc.sourceWeb of Science-
dc.subjectphospholipase A(2)pt
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.contributor.institutionUniversidade Estadual Paulista (UNESP)-
dc.contributor.institutionUniversidade de São Paulo (USP)-
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.rights.accessRightsAcesso restrito-
dc.relation.ispartofBiochemical and Biophysical Research Communications-
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

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