Molecular model of shikimate kinase from Mycobacterium tuberculosis
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Tuberculosis (TB) resurged in the late 1980s and now kills approximately 3 million people a year. The reemergence of tuberculosis as a public health threat has created a need to develop new anti-mycobacterial agents. The shikimate pathway is an attractive target for herbicides and anti-microbial agents development because it is essential in algae, higher plants, bacteria, and fungi, but absent from mammals. Homologs to enzymes in the shikimate pathway have been identified in the genome sequence of Mycobacterium tuberculosis. Among them, the shikimate kinase I encoding gene (aroK) was proposed to be present by sequence homology. Accordingly, to pave the way for structural and functional efforts towards anti-mycobacterial agents development, here we describe the molecular modeling of M. tuberculosis shikimate kinase that should provide a structural framework on which the design of specific inhibitors may be based. © 2002 Elsevier Science (USA). All rights reserved.
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Bioinformatics, Drug design, Mycobacterium tuberculosis, Shikimate kinase, Structure, bacterial enzyme, shikimate kinase, unclassified drug, beta sheet, binding site, controlled study, drug design, gene sequence, hydrogen bond, molecular model, nonhuman, priority journal, sequence alignment, sequence homology, Adenosine Diphosphate, Amino Acid Sequence, Binding Sites, Hydrogen Bonding, Magnesium, Models, Molecular, Molecular Sequence Data, Pectobacterium chrysanthemi, Phosphotransferases (Alcohol Group Acceptor), Protein Structure, Secondary, Sequence Alignment, algae, Embryophyta, Fungi, Mammalia, Mycobacterium
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Biochemical and Biophysical Research Communications, v. 295, n. 1, p. 142-148, 2002.
