|
|
| (3 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==Homology model of human Toll-like receptor 5 fitted into an electron microscopy single particle reconstruction== | | ==Homology model of human Toll-like receptor 5 fitted into an electron microscopy single particle reconstruction== |
| - | <StructureSection load='3j0a' size='340' side='right' caption='[[3j0a]], [[Resolution|resolution]] 26.00Å' scene=''> | + | <SX load='3j0a' size='340' side='right' viewer='molstar' caption='[[3j0a]], [[Resolution|resolution]] 26.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3j0a]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J0A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3J0A FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3j0a]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J0A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3J0A FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 26Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TIL3, TLR5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3j0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j0a OCA], [http://pdbe.org/3j0a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3j0a RCSB], [http://www.ebi.ac.uk/pdbsum/3j0a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3j0a ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3j0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j0a OCA], [https://pdbe.org/3j0a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3j0a RCSB], [https://www.ebi.ac.uk/pdbsum/3j0a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3j0a ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Disease == | | == Disease == |
| - | [[http://www.uniprot.org/uniprot/TLR5_HUMAN TLR5_HUMAN]] Disease susceptibility is associated with variations affecting the gene represented in this entry. | + | [https://www.uniprot.org/uniprot/TLR5_HUMAN TLR5_HUMAN] Disease susceptibility is associated with variations affecting the gene represented in this entry. |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TLR5_HUMAN 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.<ref>PMID:11323673</ref> | + | [https://www.uniprot.org/uniprot/TLR5_HUMAN 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.<ref>PMID:11323673</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 21: |
Line 21: |
| | </div> | | </div> |
| | <div class="pdbe-citations 3j0a" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 3j0a" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Toll-like Receptor 3D structures|Toll-like Receptor 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| - | </StructureSection> | + | </SX> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Kanai, R]] | + | [[Category: Large Structures]] |
| - | [[Category: Lee, P]] | + | [[Category: Kanai R]] |
| - | [[Category: Modis, Y]] | + | [[Category: Lee P]] |
| - | [[Category: Wang, H W]] | + | [[Category: Modis Y]] |
| - | [[Category: Zhou, K]] | + | [[Category: Wang HW]] |
| - | [[Category: Asymmetric homodimer]]
| + | [[Category: Zhou K]] |
| - | [[Category: Glycoprotein]]
| + | |
| - | [[Category: Immune system]]
| + | |
| - | [[Category: Leucine-rich repeat]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Toll-like receptor 5]]
| + | |
| Structural highlights
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.[1]
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ 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
- ↑ Zhou K, Kanai R, Lee P, Wang HW, Modis Y. Toll-like receptor 5 forms asymmetric dimers in the absence of flagellin. J Struct Biol. 2011 Dec 8. PMID:22173220 doi:10.1016/j.jsb.2011.12.002
|
