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| Title | Toll-like receptor 5 forms asymmetric dimers in the absence of flagellin. |
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| Journal, issue, pages | J Struct Biol, Vol. 177, Issue 2, Page 402-409, Year 2012 |
| Publish date | Dec 8, 2011 |
 Authors | Kaifeng Zhou / Ryuta Kanai / Phong Lee / Hong-Wei Wang / Yorgo Modis /  |
| PubMed Abstract | The structure of full-length human TLR5 determined by electron microscopy single-particle image reconstruction at 26Å resolution shows that TLR5 forms an asymmetric homodimer via ectodomain ...The structure of full-length human TLR5 determined by electron microscopy single-particle image reconstruction at 26Å 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. |
 External links | J Struct Biol / PubMed:22173220 |
| Methods | EM (single particle) |
| Resolution | 26.0 Å |
| Structure data | EMDB-5287: The single particle reconstruction of detergent-solubilized full-length human Toll-like receptor 5  EMDB-5288: |
| Source |
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 Keywords |  IMMUNE SYSTEM / Toll-like receptor 5 / membrane protein / leucine-rich repeat / asymmetric homodimer / glycoprotein |
