Flagellin: Difference between revisions

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== Structural highlights ==
== Structural highlights ==


Fla and TLR5 binding interface is composed in part between the long helices of Fla and the ascending lateral surface of TLR5<ref>PMID:22344444</ref>.  
<scene name='77/776389/Cv/2'>Fla and TLR5 binding interface is composed in part between the long helices of Fla and the ascending lateral surface of TLR5</scene><ref>PMID:22344444</ref>.  
</StructureSection>
</StructureSection>
== 3D Structures of flagellin ==
== 3D Structures of flagellin ==

Revision as of 15:39, 5 February 2018


Function

Flagellin (Fla) from Salmonella typhimurium is the major molecular trigger by which the pathogen activates gut epithelial proinflammatory gene expression[1]. Toll-like receptor 5 (TLR5) recognizes bacterial Fla and this association mediates the innate immune response to the bacteria[2].


Structural highlights

[3].

Glycosylated flagellin (pink, yellow) complex with TLR5 (grey, green) (PDB code 3v47)

Drag the structure with the mouse to rotate

3D Structures of flagellin3D Structures of flagellin

Updated on 05-February-2018

ReferencesReferences

  1. Zeng H, Carlson AQ, Guo Y, Yu Y, Collier-Hyams LS, Madara JL, Gewirtz AT, Neish AS. Flagellin is the major proinflammatory determinant of enteropathogenic Salmonella. J Immunol. 2003 Oct 1;171(7):3668-74. PMID:14500664
  2. Hayashi F, Smith KD, Ozinsky A, Hawn TR, Yi EC, Goodlett DR, Eng JK, Akira S, Underhill DM, Aderem A. The innate immune response to bacterial flagellin is mediated by Toll-like receptor 5. Nature. 2001 Apr 26;410(6832):1099-103. PMID:11323673 doi:http://dx.doi.org/10.1038/35074106
  3. Yoon SI, Kurnasov O, Natarajan V, Hong M, Gudkov AV, Osterman AL, Wilson IA. Structural basis of TLR5-flagellin recognition and signaling. Science. 2012 Feb 17;335(6070):859-64. PMID:22344444 doi:10.1126/science.1215584

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Michal Harel, Joel L. Sussman, Alexander Berchansky