Crystal structure of a novel cysteinless plant Kunitz-type protease inhibitor

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dc.contributor.authorHansen, Daiane
dc.contributor.authorMacedo-Ribeiro, Sandra
dc.contributor.authorVerissimo, Paula
dc.contributor.authorIm, Sonia Yoo
dc.contributor.authorSampaio, Misako Uemura
dc.contributor.authorOliva, Maria Luiza Vilela
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionUniv Coimbra
dc.contributor.institutionInst Biol Mol & Celular
dc.date.accessioned2016-01-24T13:49:05Z
dc.date.available2016-01-24T13:49:05Z
dc.date.issued2007-09-07
dc.description.abstractBauhinia bauhinioides Cruzipain Inhibitor (BbCI) is a cysteine protease inhibitor highly homologous to plant Kunitz-type inhibitors. However, in contrast to classical Kunitz family inhibitors it lacks cysteine residues and therefore disulfide bridges. BbCI is also distinct in the ability to inactivate enzymes belonging to two different classes, cysteine and serine proteases. Besides inhibiting the cysteine protease cruzipain, BbCI also inhibits cathepsin L and the serine proteases HNE (human neutrophil elastase) and PPE (porcine pancreatic elastase). Monoclinic crystals of the recombinant inhibitor that diffract to 1.7 angstrom resolution were obtained using hanging drop method by vapor diffusion at 18 degrees C. the refined structure shows the conservative P-trefoil fold features of the Kunitz inhibitors. in BbCI, one of the two characteristic S-S bonds is replaced by the water-mediated interaction between Tyr125 and Gly132. in this work we explore the structural differences between Kunitz-type inhibitors and analyze the essential interactions that maintain the protein structural stability preserving its biological function. (c) 2007 Elsevier Inc. All rights reserved.en
dc.description.affiliationUniversidade Federal de São Paulo, Escola Paulista Med, Dept Bioquim, BR-04044020 São Paulo, Brazil
dc.description.affiliationUniv Coimbra, Dept Bioquim, P-3004517 Coimbra, Portugal
dc.description.affiliationUniv Coimbra, Ctr Neurociencias & Biol Celular, P-3004517 Coimbra, Portugal
dc.description.affiliationInst Biol Mol & Celular, P-4150180 Oporto, Portugal
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Escola Paulista Med, Dept Bioquim, BR-04044020 São Paulo, Brazil
dc.description.sourceWeb of Science
dc.format.extent735-740
dc.identifierhttp://dx.doi.org/10.1016/j.bbrc.2007.06.144
dc.identifier.citationBiochemical and Biophysical Research Communications. San Diego: Academic Press Inc Elsevier Science, v. 360, n. 4, p. 735-740, 2007.
dc.identifier.doi10.1016/j.bbrc.2007.06.144
dc.identifier.issn0006-291X
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/30040
dc.identifier.wosWOS:000248502700005
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofBiochemical and Biophysical Research Communications
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.subjectcathepsinen
dc.subjectCrystallographyen
dc.subjectCruzipainen
dc.subjectelastaseen
dc.subjectKallikreinen
dc.subjectKunitz protease inhibitorsen
dc.subjectX-ray diffractionen
dc.titleCrystal structure of a novel cysteinless plant Kunitz-type protease inhibitoren
dc.typeinfo:eu-repo/semantics/article
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