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Registro Completo |
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Biblioteca(s): |
Embrapa Recursos Genéticos e Biotecnologia. |
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Data corrente: |
05/01/2011 |
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Data da última atualização: |
03/06/2024 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Autoria: |
RIBEIRO; TOGAWA, R. C.; NESHICH, I. A. P.; MAZONI, I.; MANCINI, A. L.; MINARDI, R. C. de M.; SILVEIRA, C. H. da; JARDINE, J. G.; SANTORO, M. M.; NESHICH, G. |
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Afiliação: |
CRISTINA RIBEIRO, UFMG; ROBERTO COITI TOGAWA, CENARGEN; IZABELLA A. P. NESHICH; IVAN MAZONI, CNPTIA; ADAUTO LUIZ MANCINI, CNPTIA; RAQUEL C. DE MELO MINARDI, UFMG; CARLOS H. DA SILVEIRA, UNIFEI; JOSE GILBERTO JARDINE, CNPTIA; MARCELO M. SANTORO, UFMG; GORAN NESHICH, CNPTIA. |
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Título: |
Analysis of binding properties and specificity through identification of the interface forming residues (IFR) for serine proteases in silico docked to different inhibitors. |
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Ano de publicação: |
2010 |
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Fonte/Imprenta: |
BMC Structural Biology, London, v. 10, n. 36, p. 1-16, 2010. |
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Idioma: |
Inglês |
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Notas: |
Disponível em:.Acesso em: 5 jan. 2011. |
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Conteúdo: |
Background: Enzymes belonging to the same super family of proteins in general operate on variety of substrates and are inhibited by wide selection of inhibitors. In this work our main objective was to expand the scope of studies that consider only the catalytic and binding pocket amino acids while analyzing enzyme specificity and instead, include a wider category which we have named the Interface Forming Residues (IFR). We were motivated to identify those amino acids with decreased accessibility to solvent after docking of different types of inhibitors to sub classes of serine proteases and then create a table (matrix) of all amino acid positions at the interface as well as their respective occupancies. Our goal is to establish a platform for analysis of the relationship between IFR characteristics and binding properties/specificity for bi-molecular complexes. Results: We propose a novel method for describing binding properties and delineating serine proteases specificity by compiling an exhaustive table of interface forming residues (IFR) for serine proteases and their inhibitors. Currently, the Protein Data Bank (PDB) does not contain all the data that our analysis would require. Therefore, an in silico approach was designed for building corresponding complexes The IFRs are obtained by ?rigid body docking? among 70 structurally aligned, sequence wise non-redundant, serine protease structures with 3 inhibitors: bovine pancreatic trypsin inhibitor (BPTI), ecotine and ovomucoid third domain inhibitor. The table (matrix) of all amino acid positions at the interface and their respective occupancy is created. We also developed a new computational protocol for predicting IFRs for those complexes which were not deciphered experimentally so far, achieving accuracy of at least 0.97. Conclusions: The serine proteases interfaces prefer polar (including glycine) residues (with some exceptions). Charged residues were found to be uniquely prevalent at the interfaces between the ?miscellaneous-virus? subfamily and the three inhibitors. This prompts speculation about how important this difference in IFR characteristics is for maintaining virulence of those organisms. Our work here provides a unique tool for both structure/function relationship analysis as well as a compilation of indicators detailing how the specificity of various serine proteases may have been achieved and/or could be altered. It also indicates that the interface forming residues which also determine specificity of serine protease sub-family can not be presented in a canonical way but rather as a matrix of alternative populations of amino acids occupying variety of IFR positions. MenosBackground: Enzymes belonging to the same super family of proteins in general operate on variety of substrates and are inhibited by wide selection of inhibitors. In this work our main objective was to expand the scope of studies that consider only the catalytic and binding pocket amino acids while analyzing enzyme specificity and instead, include a wider category which we have named the Interface Forming Residues (IFR). We were motivated to identify those amino acids with decreased accessibility to solvent after docking of different types of inhibitors to sub classes of serine proteases and then create a table (matrix) of all amino acid positions at the interface as well as their respective occupancies. Our goal is to establish a platform for analysis of the relationship between IFR characteristics and binding properties/specificity for bi-molecular complexes. Results: We propose a novel method for describing binding properties and delineating serine proteases specificity by compiling an exhaustive table of interface forming residues (IFR) for serine proteases and their inhibitors. Currently, the Protein Data Bank (PDB) does not contain all the data that our analysis would require. Therefore, an in silico approach was designed for building corresponding complexes The IFRs are obtained by ?rigid body docking? among 70 structurally aligned, sequence wise non-redundant, serine protease structures with 3 inhibitors: bovine pancreatic trypsin inhibitor (BPTI), ecotine and ovomuco... Mostrar Tudo |
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Palavras-Chave: |
Enzimas; Interface Forming Residues; Propriedades ligantes; Proteases. |
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Thesaurus Nal: |
Binding properties; Enzymes. |
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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/23695/1/1472-6807-10-36.pdf
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Marc: |
LEADER 03733naa a2200313 a 4500
001 1871662
005 2024-06-03
008 2010 bl uuuu u00u1 u #d
100 1 $aRIBEIRO
245 $aAnalysis of binding properties and specificity through identification of the interface forming residues (IFR) for serine proteases in silico docked to different inhibitors.$h[electronic resource]
260 $c2010
500 $aDisponível em:<http://www.biomedcentral.com/1472-6807/10/36>.Acesso em: 5 jan. 2011.
520 $aBackground: Enzymes belonging to the same super family of proteins in general operate on variety of substrates and are inhibited by wide selection of inhibitors. In this work our main objective was to expand the scope of studies that consider only the catalytic and binding pocket amino acids while analyzing enzyme specificity and instead, include a wider category which we have named the Interface Forming Residues (IFR). We were motivated to identify those amino acids with decreased accessibility to solvent after docking of different types of inhibitors to sub classes of serine proteases and then create a table (matrix) of all amino acid positions at the interface as well as their respective occupancies. Our goal is to establish a platform for analysis of the relationship between IFR characteristics and binding properties/specificity for bi-molecular complexes. Results: We propose a novel method for describing binding properties and delineating serine proteases specificity by compiling an exhaustive table of interface forming residues (IFR) for serine proteases and their inhibitors. Currently, the Protein Data Bank (PDB) does not contain all the data that our analysis would require. Therefore, an in silico approach was designed for building corresponding complexes The IFRs are obtained by ?rigid body docking? among 70 structurally aligned, sequence wise non-redundant, serine protease structures with 3 inhibitors: bovine pancreatic trypsin inhibitor (BPTI), ecotine and ovomucoid third domain inhibitor. The table (matrix) of all amino acid positions at the interface and their respective occupancy is created. We also developed a new computational protocol for predicting IFRs for those complexes which were not deciphered experimentally so far, achieving accuracy of at least 0.97. Conclusions: The serine proteases interfaces prefer polar (including glycine) residues (with some exceptions). Charged residues were found to be uniquely prevalent at the interfaces between the ?miscellaneous-virus? subfamily and the three inhibitors. This prompts speculation about how important this difference in IFR characteristics is for maintaining virulence of those organisms. Our work here provides a unique tool for both structure/function relationship analysis as well as a compilation of indicators detailing how the specificity of various serine proteases may have been achieved and/or could be altered. It also indicates that the interface forming residues which also determine specificity of serine protease sub-family can not be presented in a canonical way but rather as a matrix of alternative populations of amino acids occupying variety of IFR positions.
650 $aBinding properties
650 $aEnzymes
653 $aEnzimas
653 $aInterface Forming Residues
653 $aPropriedades ligantes
653 $aProteases
700 1 $aTOGAWA, R. C.
700 1 $aNESHICH, I. A. P.
700 1 $aMAZONI, I.
700 1 $aMANCINI, A. L.
700 1 $aMINARDI, R. C. de M.
700 1 $aSILVEIRA, C. H. da
700 1 $aJARDINE, J. G.
700 1 $aSANTORO, M. M.
700 1 $aNESHICH, G.
773 $tBMC Structural Biology, London$gv. 10, n. 36, p. 1-16, 2010.
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Registro original: |
Embrapa Recursos Genéticos e Biotecnologia (CENARGEN) |
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| Registros recuperados : 77 | |
| 2. |  | MAZONI, I.; NESHICH, G. DPIN: um dicionário dos nanoambientes internos das proteínas e seu potencial para transformação em ativos para a agricultura. In: MASSRUHÁ, S. M. F. S.; LEITE, M. A. de A.; OLIVEIRA, S. R. de M.; MEIRA, C. A. A.; LUCHIARI JUNIOR, A.; BOLFE, E. L. (Ed.). Agricultura digital: pesquisa, desenvolvimento e inovação nas cadeias produtivas. Brasília, DF: Embrapa, 2020. cap. 9, p. 218-232.| Tipo: Capítulo em Livro Técnico-Científico |
| Biblioteca(s): Embrapa Agricultura Digital. |
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| 3. | | MAZONI, I.; NESHICH, G. DIPN: a dictionary of the internal proteins nanoenvironments and their potential for transformation into agricultural assets. In: MASSRUHÁ, S. M. F. S.; LEITE, M. A. de A.; OLIVEIRA, S. R. de M.; MEIRA, C. A. A.; LUCHIARI JUNIOR, A.; BOLFE, E. L. (ed.). Digital agriculture: research, development and innovation in production chains. Brasília, DF: Embrapa, 2023. cap. 9, p. 165-177.| Tipo: Capítulo em Livro Técnico-Científico |
| Biblioteca(s): Embrapa Agricultura Digital. |
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| 10. | | NESHICH, G.; JARDINE, J. G.; BERNARDES, R.; MAZONI, I.; MANCINI, A. L.; SILVEIRA, C. da. "Cloud computation" na forma de serviços WEB para um banco de dados federativo STING_RDB. In: SIMPÓSIO SOBRE INOVAÇÃO E CRIATIVIDADE CIENTÍFICA NA EMBRAPA, 1., 2008, Brasília, DF. Comunicações Selecionadas. Brasília, DF: Embrapa, 2008. Não paginado.| Tipo: Resumo em Anais de Congresso |
| Biblioteca(s): Embrapa Agricultura Digital. |
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| 12. | | MELO, R. C.; MAZONI, I.; NESHICH, G.; SANTORO, M. M.; MEIRA JÚNIOR, W. Contacts as the key elements for comparing two protein structures. In: ANNUAL INTERNATIONAL CONFERENCE ON INTELLIGENT SYSTEMS FOR MOLECULAR BIOLOGY, 14.; ANNUAL AB3C CONFERENCE, 2., 2006, Fortaleza. Conference Program... Fortaleza: ISCB, 2006. Não paginado. ISMB, X-MEETING 2006. Poster I-6.| Tipo: Resumo em Anais de Congresso |
| Biblioteca(s): Embrapa Agricultura Digital. |
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| 13. | | MELO, R. C.; MAZONI, I.; NESHICH, G.; SANTORO, M. M.; MEIRA JUNIOR, W. Protein structure topology comparison based on contact maps. In: ANNUAL INTERNATIONAL CONFERENCE ON INTELLIGENT SYSTEMS FOR MOLECULAR BIOLOGY, 14.; ANNUAL AB3C CONFERENCE, 2., 2006, Fortaleza. Conference Program... Fortaleza: ISCB, 2006. Não paginado. ISMB, X-MEETING 2006. Poster I-5.| Tipo: Resumo em Anais de Congresso |
| Biblioteca(s): Embrapa Agricultura Digital. |
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| 14. | | JARDINE, J. G.; MAZONI, I.; BORRO, L. C.; ALVARENGA, D.; NESHICH, G. Signature contact coordination patterns for secondary structure elements in protein structures. In: ANNUAL MEETING OF SBBQ, 37.; CONGRESS OF THE PAN-AMERICAN ASSOCIATION FOR BIOCHEMISTRY AND MOLECULAR BIOLOGY, 11, 2008, Águas de Lindóia. Program and index... Águas de Lindóia: SBBq, 2008. Não paginado. PABMB.| Tipo: Resumo em Anais de Congresso |
| Biblioteca(s): Embrapa Agricultura Digital. |
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| 15. | | MAZONI, I.; JARDINE, J. G.; BORRO, L. C.; ALVARENGA, D.; NESHICH, G. Electrostatic potential at the alpha carbon atoms along the alpha helices and beta strands. In: ANNUAL MEETING OF SBBQ, 37.; CONGRESS OF THE PAN-AMERICAN ASSOCIATION FOR BIOCHEMISTRY AND MOLECULAR BIOLOGY, 11, 2008, Águas de Lindóia. Program and index... Águas de Lindóia, Program and index... Águas de Lindóia: SBBq, 2008. Não paginado. PABMB.| Tipo: Resumo em Anais de Congresso |
| Biblioteca(s): Embrapa Agricultura Digital. |
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| 16. | | SALIM, J. A.; BORRO, L.; MAZONI, I.; YANO, I. H.; JARDINE, J. G.; NESHICH, G. Multiple structure single parameter: analysis of a single protein nano environment descriptor characterizing a shared loci on structurally aligned proteins. Bioinformatics, v. 32, n. 12, p. 1885-1887, 2016.| Tipo: Artigo em Periódico Indexado | Circulação/Nível: A - 1 |
| Biblioteca(s): Embrapa Agricultura Digital. |
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| 18. | | PENA, I.; MANCINI, A. L.; MAZONI, I.; JARDINE, J. G.; NESHICH, G.; ORTEGA, J. M. Identification of philogenetic relationship between GDPD and SMaseD proteins based on active site amino acid physical chemical properties. In: INTERNATIONAL CONFERENCE OF BRAZILIAN ASSOCIATION FOR BIOINFORMATICS AND COMPUTATIONAL BIOLOGY, 4., 2008, Salvador. Proceedings... Salvador: AB³C, 2008. Não paginado. X-Meeting 2008.| Tipo: Resumo em Anais de Congresso |
| Biblioteca(s): Embrapa Agricultura Digital. |
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| 19. | | BORRO, L. C.; SALIM, J. A.; MAZONI, I.; YANO, I.; JARDINE, J. G.; NESHICH, G. Improving binding affinity prediction by using a rule-based model with physical-chemical and structural descriptors of the nano-environment for protein-ligand interactions. In: CONGRESS OF THE INTERNATIONAL UNION FOR BIOCHEMISTRY AND MOLECULAR BIOLOGY, 23.; ANNUAL MEETING OF THE BRAZILIAN SOCIETY FOR BIOCHEMISTRY AND MOLECULAR BIOLOGY, 44., 2015, Foz do Iguaçu. Biochemistry for a better world: abstracts book. [Foz do Iguaçu]: SBBq, 2015. p. 153. C.047.| Tipo: Resumo em Anais de Congresso |
| Biblioteca(s): Embrapa Agricultura Digital. |
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| Registros recuperados : 77 | |
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| Nenhum registro encontrado para a expressão de busca informada. |
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