2j67: Difference between revisions

New page: left|200px<br /> <applet load="2j67" size="450" color="white" frame="true" align="right" spinBox="true" caption="2j67, resolution 2.20Å" /> '''THE TIR DOMAIN OF H...
 
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'''THE TIR DOMAIN OF HUMAN TOLL-LIKE RECEPTOR 10 (TLR10)'''<br />


==About this Structure==
==The TIR domain of human Toll-Like Receptor 10 (TLR10)==
2J67 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2J67 OCA].  
<StructureSection load='2j67' size='340' side='right'caption='[[2j67]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2j67]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. The November 2011 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Toll-like Receptors''  by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2011_11 10.2210/rcsb_pdb/mom_2011_11]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J67 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J67 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]] 2.2&#8491;</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=2j67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j67 OCA], [https://pdbe.org/2j67 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j67 RCSB], [https://www.ebi.ac.uk/pdbsum/2j67 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j67 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TLR10_HUMAN TLR10_HUMAN] Participates in the innate immune response to microbial agents. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (By similarity).
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/j6/2j67_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2j67 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Toll/interleukin-1 receptor (TIR) domain is a highly conserved signaling domain found in the intracellular regions of Toll-like receptors (TLRs), in interleukin-1 receptors, and in several cytoplasmic adaptor proteins. TIR domains mediate receptor signal transduction through recruitment of adaptor proteins and play critical roles in the innate immune response and inflammation. This work presents the 2.2A crystal structure of the TIR domain of human TLR10, revealing a symmetric dimer in the asymmetric unit. The dimer interaction surface contains residues from the BB-loop, DD-loop, and alphaC-helix, which have previously been identified as important structural motifs for signaling in homologous TLR receptors. The interaction surface is extensive, containing a central hydrophobic patch surrounded by polar residues. The BB-loop forms a tight interaction, where a range of consecutive residues binds in a pocket formed by the reciprocal BB-loop and alphaC-helix. This pocket appears to be well suited for binding peptide substrates, which is consistent with the notion that peptides and peptide mimetics of the BB-loop are inhibitors for TLR signaling. The TLR10 structure is in good agreement with available biochemical data on TLR receptors and is likely to provide a good model for the physiological dimer.
 
The crystal structure of the human toll-like receptor 10 cytoplasmic domain reveals a putative signaling dimer.,Nyman T, Stenmark P, Flodin S, Johansson I, Hammarstrom M, Nordlund P J Biol Chem. 2008 May 2;283(18):11861-5. Epub 2008 Mar 10. PMID:18332149<ref>PMID:18332149</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2j67" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Toll-like Receptor 3D structures|Toll-like Receptor 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Arrowsmith, C.]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: Berg, S.Van.Den.]]
[[Category: Toll-like Receptors]]
[[Category: Berglund, H.]]
[[Category: Arrowsmith C]]
[[Category: Busam, R.]]
[[Category: Berglund H]]
[[Category: Collins, R.]]
[[Category: Busam R]]
[[Category: Edwards, A.]]
[[Category: Collins R]]
[[Category: Ericsson, U.B.]]
[[Category: Edwards A]]
[[Category: Flodin, S.]]
[[Category: Ericsson UB]]
[[Category: Flores, A.]]
[[Category: Flodin S]]
[[Category: Graslund, S.]]
[[Category: Flores A]]
[[Category: Hallberg, B.M.]]
[[Category: Graslund S]]
[[Category: Hammarstrom, M.]]
[[Category: Hallberg BM]]
[[Category: Hogbom, M.]]
[[Category: Hammarstrom M]]
[[Category: Johansson, I.]]
[[Category: Hogbom M]]
[[Category: Karlberg, T.]]
[[Category: Holmberg Schiavone L]]
[[Category: Kotenyova, T.]]
[[Category: Johansson I]]
[[Category: Magnusdottir, A.]]
[[Category: Karlberg T]]
[[Category: Nilsson, M.E.]]
[[Category: Kotenyova T]]
[[Category: Nilsson-Ehle, P.]]
[[Category: Magnusdottir A]]
[[Category: Nordlund, P.]]
[[Category: Nilsson ME]]
[[Category: Nyman, T.]]
[[Category: Nilsson-Ehle P]]
[[Category: Ogg, D.]]
[[Category: Nordlund P]]
[[Category: Persson, C.]]
[[Category: Nyman T]]
[[Category: Sagemark, J.]]
[[Category: Ogg D]]
[[Category: Schiavone, L.Holmberg.]]
[[Category: Persson C]]
[[Category: Stenmark, P.]]
[[Category: Sagemark J]]
[[Category: Sundstrom, M.]]
[[Category: Stenmark P]]
[[Category: Thorsell, A.G.]]
[[Category: Sundstrom M]]
[[Category: Uppenberg, J.]]
[[Category: Thorsell AG]]
[[Category: Wallden, K.]]
[[Category: Uppenberg J]]
[[Category: Weigelt, J.]]
[[Category: Van Den Berg S]]
[[Category: Welin, M.]]
[[Category: Wallden K]]
[[Category: glycoprotein]]
[[Category: Weigelt J]]
[[Category: il-1]]
[[Category: Welin M]]
[[Category: immune response]]
[[Category: inflammatory response]]
[[Category: innate immunity]]
[[Category: leucine-rich repeat]]
[[Category: membrane]]
[[Category: polymorphism]]
[[Category: receptor]]
[[Category: tir]]
[[Category: tlr10]]
[[Category: toll]]
[[Category: toll-like receptor 10]]
[[Category: transmembrane]]
 
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