Structural study of binding of flagellin by Toll-like receptor 5
Data
2003-07-01
Autores
Torquato, Ricardo 
Tipo
Artigo
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Resumo
In order to predict the binding regions within the complex formed by Toll-like receptor 5 (TLR-5) and flagellin, a complementary hydropathy between the two proteins was sought. A region common to the flagellins of Salmonella enterica serovar Typhimurium, Pseudomonas aeruginosa, and Listeria monocytogenes was shown to be hydropathically complementary to the 552-to-561 fragment of TLR-5, whose sequence is EILDISRNQL. the hydrophobicity profile of this region is shared with flagellins of 377 bacteria] species out of a total of 723 publicly available sequences. A conformational analysis of the predicted binding site of TLR-5, whose structure is still unknown, was carried out with a methodology already applied to similar problems. To sample the conformations available to the peptide chain, a plot of the number of conformations per unit energy interval (density of states) versus energy was built. Following a theoretical argument, conformations belonging to maxima in this plot were selected. the most stable structure obtained in this search, an alpha-helical conformation, was shown to form the electrostatic interactions Glu552-Gin89, Asp555-Arg92, and Arg558-Glu93 with the predicted binding site of the flagellin of S. enterica serovar Typhimurium, formed by the 88-to-97 chain fragment (LQRVRELAVQ), which is likewise alpha helical.
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Citação
Journal of Bacteriology. Washington: Amer Soc Microbiology, v. 185, n. 14, p. 4243-4247, 2003.