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dc.contributor.authorFERNANDEZ, J. H.pt_BR
dc.contributor.authorMELLO, M. Opt_BR
dc.contributor.authorGALGARO, L.pt_BR
dc.contributor.authorTANAKA, A. S.pt_BR
dc.contributor.authorSILVA-FILHO, M. C.pt_BR
dc.contributor.authorNESHICH, G.pt_BR
dc.date.accessioned2011-04-10T11:11:11Zpt_BR
dc.date.available2011-04-10T11:11:11Zpt_BR
dc.date.created2007-12-07pt_BR
dc.date.issued2007pt_BR
dc.identifier.citationGenetics and Molecular Research, v. 6, n. 4, p. 846-858, 2007.pt_BR
dc.identifier.urihttp://www.alice.cnptia.embrapa.br/alice/handle/doc/764pt_BR
dc.descriptionAbsttract . Bowman-Birk inhibitors (BBIs) are cysteine-rich and highly cross-linked small proteins that function as specific pseudosubstrates for digestive proteinases. They typically display a "double-headed" structure containing an independent proteinase-binding loop that can bind and inhibit trypsin, chymotrypsin and elastase. In the present study, we used computational biology to study the structural characteristics and dynamics of the inhibition mechanism of the small BBI loop expressing a 35-amino acid polypeptide (ChyTB2 inhibitor) which has coding region for the mutated chymotrypsin-inhibitory site of the soybean BBI. We found that in the BBI-trypsin inhibition complex, the most important interactions are salt bridges and hydrogen bonds, whereas in the BBI-chymotrypsin inhibition complex, the most important interactions are hydrophobic. At the same time, ChyTB2 mutant structure maintained the individual functional domain structure and excellent binding/inhibiting capacities for trypsin and chymotrypsin at the same time. These results were confirmed by enzyme-linked immunosorbend assay experiments. The results showed that modeling combined with molecular dynamics is an efficient method to describe, predict and then obtain new proteinase inhibitors. For such study, however, it is necessary to start from the sequence and structure of the mutant interacting relatively strongly with both trypsin and chymotrypsin for designing the small BBI-type inhibitor against proteinases.pt_BR
dc.language.isoengeng
dc.rightsopenAccesseng
dc.subjectInibidor Bowman-Birkpt_BR
dc.subjectModelagem molecularpt_BR
dc.subjectMolecular modelingpt_BR
dc.subjectEnzyme specificitypt_BR
dc.subjectBioinformáticapt_BR
dc.titleProteinase inhibition using small Bowman-Birk-type structures.pt_BR
dc.typeArtigo de periódicopt_BR
dc.date.updated2017-05-11T11:11:11Zpt_BR
dc.subject.thesagroProteínapt_BR
dc.subject.nalthesaurusModelspt_BR
dc.subject.nalthesaurusEnzyme-linked immunosorbent assaypt_BR
dc.subject.nalthesaurusBioinformaticspt_BR
riaa.ainfo.id764pt_BR
riaa.ainfo.lastupdate2017-05-11pt_BR
dc.contributor.institutionLNCC, Petrópolis, RJ; Esalq/USP; Esalq/USP; Unifesp; Esalq/USP; GORAN NESHICH, CNPTIA.pt_BR
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