Estrutura cristalográfica da Purina nucleosídeo foslorilase do Mycobacterium tuberculosis
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Data
2005-08-18
Autores
Silva, Diego Oliveira Nolasco da [UNESP]
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Universidade Estadual Paulista (Unesp)
Resumo
A Purina Nucleosídeo Fosforilase (PNP) catalisa a fosforólise de nucleosídeos de purina para suas respectivas bases e açucares (ribose ou desoxirribose) 1-fosfato. A PNP desempenha uma função central no metabolismo das purinas, normalmente operando na via de recuperação do DNA das células. Mais ainda, a PNP cliva ligações glicosídicas com inversão da configuração para produzir a-ribose 1-fosfato. Acredita-se que no organismo do Mycobacterium tuberculosis a PNP desempenha tarefas similares, o que levanta o interesse em desenvolver ciência que dê suporte para o desenvolvimento de drogas baseadas na estrutura desta proteína. A proteína é um homotrímero simétrico com um arranjo triangular das subunidades, similar às PNPs triméricas de mamíferos. Cada monômero consiste de um enovelamento a/ß formado por onze fitas ß circundadas por oito hélices a. O estudo desta PNP visa proporcionar comparações com outras estruturas, na intenção de identificar as bases estruturais de possíveis diferenças ou similaridades funcionais entre esta e outras PNPs, num esforço para desenvolver pesquisa que dê suporte para o desenho de novas drogas mais seletivas e poderosas contra a tuberculose.
The Purine nucleoside phosphorylase (PNP) catalyses the phosphorolysis of purine nucleosides to corresponding bases and ribose 1-phosphate. PNP plays a central role in purine metabolism, normally operating in the purine salvage pathway of cells. Moreover, PNP cleaves glycosidic bond with inversion of configuration to produce á-ribose 1-phosphate. It is believed that in the MtPNP is responsible for the same labor in the Mycobacterium tuberculosis organism, which arouses the interest in developing science for giving support to the development of structure based drugs. The protein is a symmetrical homotrimer with triangular arrangement of the subunits, similar to the trimeric mammalian PNPs. Each monomer consist of a á/â folding formed by eleven â sheet surrounded by eight á helices. The study of this PNP aims the possibility of caring out comparisons with other structures, in order to identify the structural basis of possible differences or functional similarities between this and other PNPs, in an effort to develop research which gives support to the design of more selective and powerful new drugs against tuberculosis.
The Purine nucleoside phosphorylase (PNP) catalyses the phosphorolysis of purine nucleosides to corresponding bases and ribose 1-phosphate. PNP plays a central role in purine metabolism, normally operating in the purine salvage pathway of cells. Moreover, PNP cleaves glycosidic bond with inversion of configuration to produce á-ribose 1-phosphate. It is believed that in the MtPNP is responsible for the same labor in the Mycobacterium tuberculosis organism, which arouses the interest in developing science for giving support to the development of structure based drugs. The protein is a symmetrical homotrimer with triangular arrangement of the subunits, similar to the trimeric mammalian PNPs. Each monomer consist of a á/â folding formed by eleven â sheet surrounded by eight á helices. The study of this PNP aims the possibility of caring out comparisons with other structures, in order to identify the structural basis of possible differences or functional similarities between this and other PNPs, in an effort to develop research which gives support to the design of more selective and powerful new drugs against tuberculosis.
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Palavras-chave
Biologia molecular, Cristalografia, Proteínas - Estrutura, Mycobacterium tuberculosis, Biofísica molecular, Purinas - Estrutura, Purina nucleosídeo fosforilase, Purine nucleoside phosphorylase, Tuberculosis
Como citar
SILVA, Diego Oliveira Nolasco da. Estrutura cristalográfica da Purina nucleosídeo foslorilase do Mycobacterium tuberculosis. 2005. 60 f. Dissertação (mestrado) - Universidade Estadual Paulista, Instituto de Biociências, Letras e Ciências Exatas, 2005.