Nolasco, D. O.Canduri, F.Pereira, J. H.Cortinoz, JRPalma, Mario Sergio [UNESP]Oliveira, J. S.Basso, L. A.de Azevedo, W. F.Santos, D. S.2014-05-202014-05-202004-11-12Biochemical and Biophysical Research Communications. San Diego: Academic Press Inc. Elsevier B.V., v. 324, n. 2, p. 789-794, 2004.0006-291Xhttp://hdl.handle.net/11449/19413Even being a bacterial purine nucleoside phosphorylase (PNP), which normally shows hexameric folding, the Mycobacterium tuberculosis PNP (MtPNP) resembles the mammalian trimeric structure. The crystal structure of the MtPNP apoenzyme was solved at 1.9 Angstrom resolution. The present work describes the first structure of MtPNP in complex with phosphate. In order to develop new insights into the rational drug design, conformational changes were profoundly analyzed and discussed. Comparisons over the binding sites were specially studied to improve the discussion about the selectivity of potential new drugs. (C) 2004 Elsevier B.V. All rights reserved.789-794engtuberculosisPNPCrystallographyapoenzymeselectivityArtigo10.1016/j.bbrc.2004.09.137WOS:000224794000046Acesso restrito2901888624506535