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

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

Author Hansen, Daiane Google Scholar
Macedo-Ribeiro, Sandra Google Scholar
Verissimo, Paula Google Scholar
Im, Sonia Yoo Google Scholar
Sampaio, Misako Uemura Google Scholar
Oliva, Maria Luiza Vilela Google Scholar
Institution Universidade Federal de São Paulo (UNIFESP)
Univ Coimbra
Inst Biol Mol & Celular
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.
Keywords cathepsin
Crystallography
Cruzipain
elastase
Kallikrein
Kunitz protease inhibitors
X-ray diffraction
Language English
Date 2007-09-07
Published in Biochemical and Biophysical Research Communications. San Diego: Academic Press Inc Elsevier Science, v. 360, n. 4, p. 735-740, 2007.
ISSN 0006-291X (Sherpa/Romeo, impact factor)
Publisher Elsevier B.V.
Extent 735-740
Origin http://dx.doi.org/10.1016/j.bbrc.2007.06.144
Access rights Closed access
Type Article
Web of Science ID WOS:000248502700005
URI http://repositorio.unifesp.br/handle/11600/30040

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