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Study of moleuclar interactions among thioredoxin/thioredoxin reductase and inhibitors and alosteric modulators the characterization of moecular interactions presents in the system Trx

Abstract

The thioredoxin belong to a large family of proteins whose members can interact and act upon a large number of target proteins (Meyer et al 2009). They catalyze redox reactions of disulfide bonds through an exchange mechanism dithiol disulfide (dithioldisulphide). This reaction involves a pair of cysteines separated by a pair of amino acids, which gives this family a motif (CxxC). The main function of thioredoxin is to reduce the disulfide bonds of the target protein. This PhD project has as main objective: to characterize the molecular interactions involved in the process: the catalysis and TrxRs TRXs and the process of docking of these proteins with ligands and allosteric modulators. As a second objective, we will use previous data to study the variations and TRXs TrxRs sequences that may have origins in specific mutations, whose alleles are associated with specific diseases, in order to perform binding studies of inhibitors / modulators in the mutated versions. The characterization of these molecular interactions take into account global and local conformational changes. The research project contributes to the area of molecular modeling and drug design (AU)

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VEICULO: TITULO (DATA)
VEICULO: TITULO (DATA)

Scientific publications
(References retrieved automatically from Web of Science and SciELO through information on FAPESP grants and their corresponding numbers as mentioned in the publications by the authors)
PHILOT, ERIC ALLISON; LOPES, DAVID DA MATA; DE SOUZA, ARYANE TOFANELLO; KIMUS BRAZ, ANTONIO SERGIO; NANTES, ISELI LOURENCO; RODRIGUES, TIAGO; PERAHIA, DAVID; MITEVA, MARIA A.; BARBOUR SCOTT, LUIS PAULO. Binding of phenothiazines into allosteric hydrophobic pocket of human thioredoxin 1. EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS, v. 45, n. 3, p. 279-286, . (12/07456-7, 11/11857-4, 12/12247-8)

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