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dc.contributor.authorWatanabe, L.
dc.contributor.authorSoares, A. M.
dc.contributor.authorWard, R. J.
dc.contributor.authorFontes, MRM
dc.contributor.authorArni, R. K.
dc.date.accessioned2014-05-20T13:49:23Z
dc.date.available2014-05-20T13:49:23Z
dc.date.issued2005-02-01
dc.identifierhttp://dx.doi.org/10.1016/j.biochi.2004.11.005
dc.identifier.citationBiochimie. Paris: Editions Scientifiques Medicales Elsevier, v. 87, n. 2, p. 161-167, 2005.
dc.identifier.issn0300-9084
dc.identifier.urihttp://hdl.handle.net/11449/17598
dc.description.abstractThe crystal structure of dimeric Lys49-phospholipase A2 myotoxin-II from Bothrops moojeni (MjTX-II) co-crystallized with stearic acid (C18H36O2) has been determined at a resolution of 1.8 angstrom. The electron density maps permitted the unambiguous inclusion of six stearic acid molecules in the refinement. Two stearic acid molecules could be located in the substrate-binding cleft of each monomer in positions, which favor the interaction of their carboxyl groups with active site residues. The way of binding of stearic acids to this Lys49-PLA(2)s is analogous to phospholipids and transition state analogues to catalytically active PLA(2)s. Two additional stearic acid molecules were located at the dimer interface region, defining a hitherto unidentified acyl-binding site on the protein surface. The strictly conserved Lys122 for Lys49-PLA(2)s may play a fundamental role for stabilization of legend-protein complex. The comparison of MjTX-II/satiric acid complex with other Lys-PLA(2)s structures whose putative fatty acids were located at their active site is also analysed. Molecular details of the stearic acid/protein interactions provide insights to binding in croup I/II PLA(2)s and to the possible interactions of Lys49-PLA(2)s with target membranes. (c) 2004 Elsevier SAS. All rights reserved.en
dc.format.extent161-167
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofBiochimie
dc.sourceWeb of Science
dc.subjectphospholipase A(2)pt
dc.subjectstearic acidpt
dc.subjectCrystal structurept
dc.subjectdimer interface fatty acid bindingpt
dc.titleStructural insights for fatty acid binding in a Lys49-phospholipase A(2): crystal structure of myotoxin II from Bothrops molojeni complexed with stearic aciden
dc.typeArtigo
dcterms.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dcterms.rightsHolderElsevier B.V.
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)
dc.contributor.institutionUNAERP
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.description.affiliationUNESP, IBILCE, Dept Fis, Sao Jose do Rio Preto, SP, Brazil
dc.description.affiliationUNAERP, Unidade Biotecnol, Ribeirao Preto, SP, Brazil
dc.description.affiliationUSP, FFCLRP, Dept Quim, Ribeirao Preto, SP, Brazil
dc.description.affiliationUniv Estadual Paulista Julio Mesquita Filho, Inst Biociencias, Dept Fis & Biofis, Botucatu, SP, Brazil
dc.description.affiliationUnespUNESP, IBILCE, Dept Fis, Sao Jose do Rio Preto, SP, Brazil
dc.description.affiliationUnespUniv Estadual Paulista Julio Mesquita Filho, Inst Biociencias, Dept Fis & Biofis, Botucatu, SP, Brazil
dc.identifier.doi10.1016/j.biochi.2004.11.005
dc.identifier.wosWOS:000227845100004
dc.rights.accessRightsAcesso restrito
unesp.campusUniversidade Estadual Paulista (UNESP), Instituto de Biociências, Botucatupt
unesp.campusUniversidade Estadual Paulista (UNESP), Instituto de Biociências Letras e Ciências Exatas, São José do Rio Pretopt
dc.identifier.lattes9162508978945887
unesp.author.lattes9162508978945887
unesp.author.orcid0000-0002-4634-6221[4]
unesp.author.orcid0000-0003-1136-5737[3]
dc.relation.ispartofjcr3.188
dc.relation.ispartofsjr1,554
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