3v44: Difference between revisions
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The | ==Crystal structure of the N-terminal fragment of zebrafish TLR5== | ||
<StructureSection load='3v44' size='340' side='right'caption='[[3v44]], [[Resolution|resolution]] 2.83Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3v44]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Danio_rerio Danio rerio] and [https://en.wikipedia.org/wiki/Eptatretus_burgeri Eptatretus burgeri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V44 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3V44 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.83Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=3v44 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v44 OCA], [https://pdbe.org/3v44 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3v44 RCSB], [https://www.ebi.ac.uk/pdbsum/3v44 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3v44 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/B3DIN1_DANRE B3DIN1_DANRE] [https://www.uniprot.org/uniprot/Q4G1L2_EPTBU Q4G1L2_EPTBU] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Toll-like receptor 5 (TLR5) binding to bacterial flagellin activates signaling through the transcription factor NF-kappaB and triggers an innate immune response to the invading pathogen. To elucidate the structural basis and mechanistic implications of TLR5-flagellin recognition, we determined the crystal structure of zebrafish TLR5 (as a variable lymphocyte receptor hybrid protein) in complex with the D1/D2/D3 fragment of Salmonella flagellin, FliC, at 2.47 angstrom resolution. TLR5 interacts primarily with the three helices of the FliC D1 domain using its lateral side. Two TLR5-FliC 1:1 heterodimers assemble into a 2:2 tail-to-tail signaling complex that is stabilized by quaternary contacts of the FliC D1 domain with the convex surface of the opposing TLR5. The proposed signaling mechanism is supported by structure-guided mutagenesis and deletion analyses on CBLB502, a therapeutic protein derived from FliC. | |||
Structural basis of TLR5-flagellin recognition and signaling.,Yoon SI, Kurnasov O, Natarajan V, Hong M, Gudkov AV, Osterman AL, Wilson IA Science. 2012 Feb 17;335(6070):859-64. PMID:22344444<ref>PMID:22344444</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3v44" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Toll-like Receptor 3D structures|Toll-like Receptor 3D structures]] | |||
*[[Variable lymphocyte receptor 3D structures|Variable lymphocyte receptor 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Danio rerio]] | |||
[[Category: Eptatretus burgeri]] | |||
[[Category: Large Structures]] | |||
[[Category: Hong H]] | |||
[[Category: Wilson IA]] | |||
[[Category: Yoon SI]] | |||
Latest revision as of 09:15, 17 October 2024
Crystal structure of the N-terminal fragment of zebrafish TLR5Crystal structure of the N-terminal fragment of zebrafish TLR5
Structural highlights
FunctionPublication Abstract from PubMedToll-like receptor 5 (TLR5) binding to bacterial flagellin activates signaling through the transcription factor NF-kappaB and triggers an innate immune response to the invading pathogen. To elucidate the structural basis and mechanistic implications of TLR5-flagellin recognition, we determined the crystal structure of zebrafish TLR5 (as a variable lymphocyte receptor hybrid protein) in complex with the D1/D2/D3 fragment of Salmonella flagellin, FliC, at 2.47 angstrom resolution. TLR5 interacts primarily with the three helices of the FliC D1 domain using its lateral side. Two TLR5-FliC 1:1 heterodimers assemble into a 2:2 tail-to-tail signaling complex that is stabilized by quaternary contacts of the FliC D1 domain with the convex surface of the opposing TLR5. The proposed signaling mechanism is supported by structure-guided mutagenesis and deletion analyses on CBLB502, a therapeutic protein derived from FliC. Structural basis of TLR5-flagellin recognition and signaling.,Yoon SI, Kurnasov O, Natarajan V, Hong M, Gudkov AV, Osterman AL, Wilson IA Science. 2012 Feb 17;335(6070):859-64. PMID:22344444[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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