Structural bioinformatics study of PNP from Schistosoma mansoni

dc.contributorPontifícia Universidade Católica do Rio Grande do Sul (PUCRS)
dc.contributorUniversidade Estadual Paulista (Unesp)
dc.contributorUniversidade Federal do Rio Grande do Sul (UFRGS)
dc.contributorInstituto Butantan
dc.date.accessioned2014-05-20T13:54:25Z
dc.date.available2014-05-20T13:54:25Z
dc.date.created2014-05-20T13:54:25Z
dc.date.issued2004-09-10
dc.identifierBiochemical and Biophysical Research Communications. San Diego: Academic Press Inc. Elsevier B.V., v. 322, n. 1, p. 100-104, 2004.
dc.identifier0006-291X
dc.identifierhttp://hdl.handle.net/11449/19454
dc.identifier10.1016/j.bbrc.2004.07.088
dc.identifierWOS:000223581000015
dc.identifier2901888624506535
dc.description.abstractThe parasite Schistosoma mansoni lacks the de novo pathway for purine biosynthesis and depends on salvage pathways for its purine requirements. Schistosomiasis is endemic in 76 countries and territories and amongst the parasitic diseases ranks second after malaria in terms of social and economic impact and public health importance. The PNP is an attractive target for drug design and it has been submitted to extensive structure-based design. The atomic coordinates of the complex of human PNP with inosine were used as template for starting the modeling of PNP from S. mansoni complexed with inosine. Here we describe the model for the complex SmPNP-inosine and correlate the structure with differences in the affinity for inosine presented by human and S. mansoni PNPs. (C) 2004 Elsevier B.V. All rights reserved.
dc.languageeng
dc.publisherElsevier B.V.
dc.relationBiochemical and Biophysical Research Communications
dc.relation2.559
dc.rightsAcesso restrito
dc.sourceWeb of Science
dc.subjectstructural bioinformatics
dc.subjectSchistosoma mansoni
dc.subjectPNP
dc.subjectdrug design
dc.titleStructural bioinformatics study of PNP from Schistosoma mansoni
dc.typeArtículos de revistas


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