Molecular model of shikimate kinase from Mycobacterium tuberculosis


Autoria(s): De Azevedo Jr., Walter Filgueira; Canduri, Fernanda; De Oliveira, Jaim Simões; Basso, Luiz Augusto; Palma, Mario Sergio; Pereihenrra, José Henrique; Santos, Diógenes Santiago
Contribuinte(s)

Universidade Estadual Paulista (UNESP)

Data(s)

27/05/2014

27/05/2014

18/07/2002

Resumo

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.

Formato

142-148

Identificador

http://dx.doi.org/10.1016/S0006-291X(02)00632-0

Biochemical and Biophysical Research Communications, v. 295, n. 1, p. 142-148, 2002.

0006-291X

http://hdl.handle.net/11449/66936

10.1016/S0006-291X(02)00632-0

WOS:000176815700025

2-s2.0-0036304185

Idioma(s)

eng

Relação

Biochemical and Biophysical Research Communications

Direitos

closedAccess

Palavras-Chave #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
Tipo

info:eu-repo/semantics/article