3J0A
Homology model of human Toll-like receptor 5 fitted into an electron microscopy single particle reconstruction
Summary for 3J0A
| Entry DOI | 10.2210/pdb3j0a/pdb |
| EMDB information | 5287 5288 |
| Descriptor | Toll-like receptor 5, alpha-L-fucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose (2 entities in total) |
| Functional Keywords | toll-like receptor 5, membrane protein, leucine-rich repeat, asymmetric homodimer, glycoprotein, immune system |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 2 |
| Total formula weight | 198455.62 |
| Authors | Modis, Y.,Zhou, K.,Kanai, R.,Lee, P.,Wang, H.W. (deposition date: 2011-06-02, release date: 2011-12-28, Last modification date: 2024-11-20) |
| Primary citation | Zhou, K.,Kanai, R.,Lee, P.,Wang, H.W.,Modis, Y. Toll-like receptor 5 forms asymmetric dimers in the absence of flagellin. J.Struct.Biol., 177:402-409, 2012 Cited by 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 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. PubMed: 22173220DOI: 10.1016/j.jsb.2011.12.002 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (26 Å) |
Structure validation
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