1P95 Protein Binding date May 09, 2003
title A Structural Study Of The Binding Of Flagellin By Toll-Like Receptor 5
authors S.G.Jacchieri, R.Torquato, R.R.Brentani
compound source
Molecule: Flagellin
Chain: A
Fragment: Residues 56-450
Synonym: Phase-1-I Flagellin
 Organism_scientific: Salmonella Typhimurium
Organism_common: Bacteria

Molecule: Toll-Like Receptor 5
Chain: B
Fragment: Fragment Predicted To Bind Flagellin
Synonym: Tollinterleukin-1 Receptor-Like Protein 3
Organism_scientific: Homo Sapiens
Organism_common: Human
methodTheoretical Model
similarity Contains 1 tir domain. Belongs to the bacterial flagellin family. Belongs to the toll-like receptor family. Contains 15 lrr (leucine-rich) repeats.[LRRCT]
subunit Binds myd88 via their respective tir domains (by similarity).
polymorphism This polymorphism acts in a dominant fashion and is associated with susceptibility to pneumonia caused by legionella pneumophila [mim. 608556]. Individuals with a stop codon polymorphism in position 352 are unable to mediate flagellin signaling.
tissue Highly expressed in ovary and in peripheral blood leukocytes, specially in monocytes, less in cd11c+ immature dendritic cells. Also detected in prostate and testis.
subcellular loc. Membrane; single-pass type i membrane protein (by similarity).
function Acts via myd88 and traf6, leading to nf-kappa-b activation, cytokine secretion and the inflammatory response. Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. Mediates detection of bacterial flagellins. Participates in the innate immune response to microbial agents.
Data retrieval
  • Asymmetric unit, PDB entry: [header only] [complete with coordinates] (53 Kb) [Save to disk]
  • CSU: Contacts of Structural Units for 1P95
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  • InterPro: IPR000483 , IPR003591 , IPR001611 , IPR000157 , IPR001492 , IPR001029
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