dc.contributor | Universidade Federal do Ceará (UFC) | |
dc.contributor | Universidade Estadual Paulista (Unesp) | |
dc.contributor | Universidade Regional Do Cariri | |
dc.contributor | Pontifícia Universidade Católica do Rio Grande do Sul (PUCRS) | |
dc.contributor | CSIC | |
dc.contributor | Université des Sciences et Technologies de Lille | |
dc.contributor | Universidade Estadual de Campinas (UNICAMP) | |
dc.contributor | Bâtiment C-9 | |
dc.date.accessioned | 2014-05-27T11:21:57Z | |
dc.date.accessioned | 2022-10-05T18:02:49Z | |
dc.date.available | 2014-05-27T11:21:57Z | |
dc.date.available | 2022-10-05T18:02:49Z | |
dc.date.created | 2014-05-27T11:21:57Z | |
dc.date.issued | 2006-09-01 | |
dc.identifier | FEBS Journal, v. 273, n. 17, p. 3962-3974, 2006. | |
dc.identifier | 1742-464X | |
dc.identifier | 1742-4658 | |
dc.identifier | http://hdl.handle.net/11449/69060 | |
dc.identifier | 10.1111/j.1742-4658.2006.05400.x | |
dc.identifier | 2-s2.0-33747413686 | |
dc.identifier | 2-s2.0-33747413686.pdf | |
dc.identifier.uri | http://repositorioslatinoamericanos.uchile.cl/handle/2250/3918555 | |
dc.description.abstract | Parkia platycephala lectin 2 was purified from Parkia platycephala (Leguminosae, Mimosoideae) seeds by affinity chromatography and RP-HPLC. Equilibrium sedimentation and MS showed that Parkia platycephala lectin 2 is a nonglycosylated monomeric protein of molecular mass 29 407 ± 15 Da, which contains six cysteine residues engaged in the formation of three intramolecular disulfide bonds. Parkia platycephala lectin 2 agglutinated rabbit erythrocytes, and this activity was specifically inhibited by N-acetylglucosamine. In addition, Parkia platycephala lectin 2 hydrolyzed β(1-4) glycosidic bonds linking 2-acetoamido-2-deoxy-β-d-glucopyranose units in chitin. The full-length amino acid sequence of Parkia platycephala lectin 2, determined by N-terminal sequencing and cDNA cloning, and its three-dimensional structure, established by X-ray crystallography at 1.75 Å resolution, showed that Parkia platycephala lectin 2 is homologous to endochitinases of the glycosyl hydrolase family 18, which share the (βα) 8 barrel topology harboring the catalytic residues Asp125, Glu127, and Tyr182. © 2006 The Authors. | |
dc.language | eng | |
dc.relation | FEBS Journal | |
dc.relation | 4.530 | |
dc.rights | Acesso aberto | |
dc.source | Scopus | |
dc.subject | Endochitinase | |
dc.subject | Glycosyl hydrolase family 18 | |
dc.subject | Mimosoideae | |
dc.subject | Parkia platycephala | |
dc.subject | X-ray crystal structure | |
dc.subject | chitin | |
dc.subject | chitinase | |
dc.subject | complementary DNA | |
dc.subject | endochitinase | |
dc.subject | genomic DNA | |
dc.subject | glycosidase | |
dc.subject | hemagglutinin | |
dc.subject | lectin | |
dc.subject | lectin 2 | |
dc.subject | n acetylglucosamine | |
dc.subject | RNA | |
dc.subject | unclassified drug | |
dc.subject | affinity chromatography | |
dc.subject | amino acid composition | |
dc.subject | amino acid sequence | |
dc.subject | animal cell | |
dc.subject | anion exchange chromatography | |
dc.subject | controlled study | |
dc.subject | crystal structure | |
dc.subject | disulfide bond | |
dc.subject | enzyme activity | |
dc.subject | enzyme analysis | |
dc.subject | enzyme inhibition | |
dc.subject | enzyme purification | |
dc.subject | erythrocyte | |
dc.subject | hemagglutination | |
dc.subject | legume | |
dc.subject | matrix assisted laser desorption ionization time of flight mass spectrometry | |
dc.subject | molecular cloning | |
dc.subject | molecular weight | |
dc.subject | nonhuman | |
dc.subject | polyacrylamide gel electrophoresis | |
dc.subject | priority journal | |
dc.subject | rabbit | |
dc.subject | reversed phase high performance liquid chromatography | |
dc.subject | RNA isolation | |
dc.subject | sedimentation | |
dc.subject | X ray crystallography | |
dc.subject | Acetylglucosamine | |
dc.subject | Amino Acid Sequence | |
dc.subject | Base Sequence | |
dc.subject | Chitinase | |
dc.subject | Cloning, Molecular | |
dc.subject | Crystallization | |
dc.subject | Crystallography, X-Ray | |
dc.subject | DNA, Complementary | |
dc.subject | Fabaceae | |
dc.subject | Hemagglutinins | |
dc.subject | Molecular Sequence Data | |
dc.subject | Plant Lectins | |
dc.subject | Protein Binding | |
dc.subject | Seeds | |
dc.subject | Oryctolagus cuniculus | |
dc.title | cDNA cloning and 1.75 Å crystal structure determination of PPL2, an endochitinase and N-acetylglucosamine-binding hemagglutinin from Parkia platycephala seeds | |
dc.type | Artigo | |