3j0a

Homology model of human Toll-like receptor 5 fitted into an electron microscopy single particle reconstructionHomology model of human Toll-like receptor 5 fitted into an electron microscopy single particle reconstruction

3j0a, resolution 26.00Å Show:Asymmetric Unit Biological Assembly Structural highlights 3j0a is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 26Å Ligands: Experimental data: Check Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease TLR5_HUMAN Disease susceptibility is associated with variations affecting the gene represented in this entry. Function TLR5_HUMAN Participates in the innate immune response to microbial agents. Mediates detection of bacterial flagellins. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. Publication Abstract from PubMed The structure of full-length human TLR5 determined by electron microscopy single-particle image reconstruction at 26A resolution shows that TLR5 forms an asymmetric homodimer via ectodomain interactions. The structure shows that like TLR9, TLR5 dimerizes in the absence of ligand. The asymmetry of the dimer suggests that TLR5 may recognize two flagellin molecules cooperatively to establish an optimal flagellin response threshold. A TLR5 homology model was generated and fitted into the electron microscopy structure. All seven predicted N-linked glycosylation sites are exposed on the molecular surface, away from the dimer interface. Glycosylation at the first five sites was confirmed by tandem mass spectrometry. Two aspartate residues proposed to interact with flagellin (Asp294 and Asp366) are sterically occluded by a glycan at position 342. In contrast, the central region of the ectodomains near the dimer interface is unobstructed by glycans. Ligand binding in this region would be consistent with the ligand binding sites of other TLRs. Toll-like receptor 5 forms asymmetric dimers in the absence of flagellin.,Zhou K, Kanai R, Lee P, Wang HW, Modis Y J Struct Biol. 2011 Dec 8. PMID:22173220 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Toll-like Receptor 3D structures