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

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dc.contributor.author Hansen, Daiane
dc.contributor.author Macedo-Ribeiro, Sandra
dc.contributor.author Verissimo, Paula
dc.contributor.author Im, Sonia Yoo
dc.contributor.author Sampaio, Misako Uemura
dc.contributor.author Oliva, Maria Luiza Vilela
dc.date.accessioned 2016-01-24T13:49:05Z
dc.date.available 2016-01-24T13:49:05Z
dc.date.issued 2007-09-07
dc.identifier http://dx.doi.org/10.1016/j.bbrc.2007.06.144
dc.identifier.citation Biochemical and Biophysical Research Communications. San Diego: Academic Press Inc Elsevier Science, v. 360, n. 4, p. 735-740, 2007.
dc.identifier.issn 0006-291X
dc.identifier.uri http://repositorio.unifesp.br/handle/11600/30040
dc.description.abstract Bauhinia 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.format.extent 735-740
dc.language.iso eng
dc.publisher Elsevier B.V.
dc.relation.ispartof Biochemical and Biophysical Research Communications
dc.rights Acesso restrito
dc.subject cathepsin en
dc.subject Crystallography en
dc.subject Cruzipain en
dc.subject elastase en
dc.subject Kallikrein en
dc.subject Kunitz protease inhibitors en
dc.subject X-ray diffraction en
dc.title Crystal structure of a novel cysteinless plant Kunitz-type protease inhibitor en
dc.type Artigo
dc.rights.license http://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.contributor.institution Universidade Federal de São Paulo (UNIFESP)
dc.contributor.institution Univ Coimbra
dc.contributor.institution Inst Biol Mol & Celular
dc.description.affiliation Universidade Federal de São Paulo, Escola Paulista Med, Dept Bioquim, BR-04044020 São Paulo, Brazil
dc.description.affiliation Univ Coimbra, Dept Bioquim, P-3004517 Coimbra, Portugal
dc.description.affiliation Univ Coimbra, Ctr Neurociencias & Biol Celular, P-3004517 Coimbra, Portugal
dc.description.affiliation Inst Biol Mol & Celular, P-4150180 Oporto, Portugal
dc.description.affiliationUnifesp Universidade Federal de São Paulo, Escola Paulista Med, Dept Bioquim, BR-04044020 São Paulo, Brazil
dc.identifier.doi 10.1016/j.bbrc.2007.06.144
dc.description.source Web of Science
dc.identifier.wos WOS:000248502700005



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