3w3l: Difference between revisions

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==Crystal structure of human TLR8 in complex with Resiquimod (R848) crystal form 1==
==Crystal structure of human TLR8 in complex with Resiquimod (R848) crystal form 1==
<StructureSection load='3w3l' size='340' side='right' caption='[[3w3l]], [[Resolution|resolution]] 2.33&Aring;' scene=''>
<StructureSection load='3w3l' size='340' side='right' caption='[[3w3l]], [[Resolution|resolution]] 2.33&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3w3l]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W3L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3W3L FirstGlance]. <br>
<table><tr><td colspan='2'>[[3w3l]] is a 4 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=3W3L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3W3L FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=RX8:1-[4-AMINO-2-(ETHOXYMETHYL)-1H-IMIDAZO[4,5-C]QUINOLIN-1-YL]-2-METHYLPROPAN-2-OL'>RX8</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=RX8:1-[4-AMINO-2-(ETHOXYMETHYL)-1H-IMIDAZO[4,5-C]QUINOLIN-1-YL]-2-METHYLPROPAN-2-OL'>RX8</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3w3g|3w3g]], [[3w3j|3w3j]], [[3w3k|3w3k]], [[3w3m|3w3m]], [[3w3n|3w3n]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3w3g|3w3g]], [[3w3j|3w3j]], [[3w3k|3w3k]], [[3w3m|3w3m]], [[3w3n|3w3n]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TLR8, UNQ249/PRO286 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TLR8, UNQ249/PRO286 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3w3l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w3l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3w3l RCSB], [http://www.ebi.ac.uk/pdbsum/3w3l PDBsum]</span></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=3w3l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w3l OCA], [http://pdbe.org/3w3l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3w3l RCSB], [http://www.ebi.ac.uk/pdbsum/3w3l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3w3l ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
Line 18: Line 19:
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 3w3l" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Human]]
[[Category: Ohto, U]]
[[Category: Ohto, U]]
[[Category: Shimizu, T]]
[[Category: Shimizu, T]]

Revision as of 18:20, 4 August 2016

Crystal structure of human TLR8 in complex with Resiquimod (R848) crystal form 1Crystal structure of human TLR8 in complex with Resiquimod (R848) crystal form 1

Structural highlights

3w3l is a 4 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , , ,
Gene:TLR8, UNQ249/PRO286 (HUMAN)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[TLR8_HUMAN] Key component of innate and adaptive immunity. TLRs (Toll-like receptors) control host immune response against pathogens through recognition of molecular patterns specific to microorganisms. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response.[1]

Publication Abstract from PubMed

Toll-like receptor 7 (TLR7) and TLR8 recognize single-stranded RNA and initiate innate immune responses. Several synthetic agonists of TLR7-TLR8 display novel therapeutic potential; however, the molecular basis for ligand recognition and activation of signaling by TLR7 or TLR8 is largely unknown. In this study, the crystal structures of unliganded and ligand-induced activated human TLR8 dimers were elucidated. Ligand recognition was mediated by a dimerization interface formed by two protomers. Upon ligand stimulation, the TLR8 dimer was reorganized such that the two C termini were brought into proximity. The loop between leucine-rich repeat 14 (LRR14) and LRR15 was cleaved; however, the N- and C-terminal halves remained associated and contributed to ligand recognition and dimerization. Thus, ligand binding induces reorganization of the TLR8 dimer, which enables downstream signaling processes.

Structural reorganization of the Toll-like receptor 8 dimer induced by agonistic ligands.,Tanji H, Ohto U, Shibata T, Miyake K, Shimizu T Science. 2013 Mar 22;339(6126):1426-9. doi: 10.1126/science.1229159. PMID:23520111[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Doyle SL, Jefferies CA, Feighery C, O'Neill LA. Signaling by Toll-like receptors 8 and 9 requires Bruton's tyrosine kinase. J Biol Chem. 2007 Dec 21;282(51):36953-60. Epub 2007 Oct 11. PMID:17932028 doi:10.1074/jbc.M707682200
  2. Tanji H, Ohto U, Shibata T, Miyake K, Shimizu T. Structural reorganization of the Toll-like receptor 8 dimer induced by agonistic ligands. Science. 2013 Mar 22;339(6126):1426-9. doi: 10.1126/science.1229159. PMID:23520111 doi:http://dx.doi.org/10.1126/science.1229159

3w3l, resolution 2.33Å

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