Registro Completo
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Biblioteca(s): |
Embrapa Agricultura Digital. |
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Data corrente: |
07/12/2007 |
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Data da última atualização: |
11/05/2017 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Circulação/Nível: |
Internacional - A |
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Autoria: |
FERNANDEZ, J. H.; MELLO, M. O; GALGARO, L.; TANAKA, A. S.; SILVA-FILHO, M. C.; NESHICH, G. |
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Afiliação: |
LNCC, Petrópolis, RJ; Esalq/USP; Esalq/USP; Unifesp; Esalq/USP; GORAN NESHICH, CNPTIA. |
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Título: |
Proteinase inhibition using small Bowman-Birk-type structures. |
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Ano de publicação: |
2007 |
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Fonte/Imprenta: |
Genetics and Molecular Research, v. 6, n. 4, p. 846-858, 2007. |
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Idioma: |
Inglês |
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Conteúdo: |
Absttract . 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. MenosAbsttract . 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 proteinas... Mostrar Tudo |
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Palavras-Chave: |
Bioinformática; Enzyme specificity; Inibidor Bowman-Birk; Modelagem molecular; Molecular modeling. |
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Thesagro: |
Proteína. |
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Thesaurus NAL: |
Bioinformatics; Enzyme-linked immunosorbent assay; Models. |
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Categoria do assunto: |
X Pesquisa, Tecnologia e Engenharia |
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URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/159697/1/AP-Proteinase-GMR-2007.pdf
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Marc: |
LEADER 02330naa a2200289 a 4500
001 1000764
005 2017-05-11
008 2007 bl uuuu u00u1 u #d
100 1 $aFERNANDEZ, J. H.
245 $aProteinase inhibition using small Bowman-Birk-type structures.$h[electronic resource]
260 $c2007
520 $aAbsttract . 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.
650 $aBioinformatics
650 $aEnzyme-linked immunosorbent assay
650 $aModels
650 $aProteína
653 $aBioinformática
653 $aEnzyme specificity
653 $aInibidor Bowman-Birk
653 $aModelagem molecular
653 $aMolecular modeling
700 1 $aMELLO, M. O
700 1 $aGALGARO, L.
700 1 $aTANAKA, A. S.
700 1 $aSILVA-FILHO, M. C.
700 1 $aNESHICH, G.
773 $tGenetics and Molecular Research$gv. 6, n. 4, p. 846-858, 2007.
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Registro original: |
Embrapa Agricultura Digital (CNPTIA) |
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