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5gy2
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of a complex between Bacillus subtilis flagellin and zebrafish Toll-like receptor 5== | |
| + | <StructureSection load='5gy2' size='340' side='right' caption='[[5gy2]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5gy2]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GY2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5GY2 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</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=5gy2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gy2 OCA], [http://pdbe.org/5gy2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5gy2 RCSB], [http://www.ebi.ac.uk/pdbsum/5gy2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5gy2 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/E0U497_BACPZ E0U497_BACPZ]] Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella.[RuleBase:RU362073] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Flagellin is a bacterial protein that polymerizes into the flagellar filament and is essential for bacterial motility. When flagellated bacteria invade the host, flagellin is recognized by Toll-like receptor 5 (TLR5) as a pathogen invasion signal and eventually evokes the innate immune response. Here, we provide a conserved structural mechanism by which flagellins from Gram-negative gamma-proteobacteria and Gram-positive Firmicutes bacteria bind and activate TLR5. The comparative structural analysis using our crystal structure of a complex between Bacillus subtilis flagellin (bsflagellin) and TLR5 at 2.1 A resolution, combined with the alanine scanning analysis of the binding interface, reveals a common hot spot in flagellin for TLR5 activation. An arginine residue (bsflagellin R89) of the flagellin D1 domain and its adjacent residues (bsflagellin E114 and L93) constitute a hot spot that provides shape and chemical complementarity to a cavity generated by the loop of leucine-rich repeat 9 in TLR5. In addition to the flagellin D1 domain, the D0 domain also contributes to TLR5 activity through structurally dispersed regions, but not a single focal area. These results establish the groundwork for the future design of flagellin-based therapeutics. | ||
| - | + | A conserved TLR5 binding and activation hot spot on flagellin.,Song WS, Jeon YJ, Namgung B, Hong M, Yoon SI Sci Rep. 2017 Jan 20;7:40878. doi: 10.1038/srep40878. PMID:28106112<ref>PMID:28106112</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5gy2" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Song, W S]] | ||
| + | [[Category: Yoon, S I]] | ||
| + | [[Category: Bacterial protein immune receptor]] | ||
| + | [[Category: Immune system]] | ||
Revision as of 17:37, 10 March 2017
Crystal structure of a complex between Bacillus subtilis flagellin and zebrafish Toll-like receptor 5
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