Please use this identifier to cite or link to this item:
|Title:||Structural study of binding of flagellin by Toll-like receptor 5|
|Authors:||Jacchieri, Saul G.|
Torquato, Ricardo [UNIFESP]
Brentani, Ricardo R.
Fundacao Antonio Prudente
Ludwig Inst Canc Res
Universidade Federal de São Paulo (UNIFESP)
|Publisher:||Amer Soc Microbiology|
|Citation:||Journal of Bacteriology. Washington: Amer Soc Microbiology, v. 185, n. 14, p. 4243-4247, 2003.|
|Abstract:||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.|
|Appears in Collections:||Em verificação - Geral|
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.