1fyv: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-{{Seed}}
-[[Image:1fyv.png|left|200px]]
-<!--
+==CRYSTAL STRUCTURE OF THE TIR DOMAIN OF HUMAN TLR1==
-The line below this paragraph, containing "STRUCTURE_1fyv", creates the "Structure Box" on the page.
+<StructureSection load='1fyv' size='340' side='right'caption='[[1fyv]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1fyv]] is a 1 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=1FYV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FYV FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-{{STRUCTURE_1fyv|  PDB=1fyv  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fyv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fyv OCA], [https://pdbe.org/1fyv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fyv RCSB], [https://www.ebi.ac.uk/pdbsum/1fyv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fyv ProSAT]</span></td></tr>
+</table>
+== 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/fy/1fyv_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1fyv ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Toll-like receptors (TLRs) and the interleukin-1 receptor superfamily (IL-1Rs) are integral to both innate and adaptive immunity for host defence. These receptors share a conserved cytoplasmic domain, known as the TIR domain. A single-point mutation in the TIR domain of murine TLR4 (Pro712His, the Lps(d) mutation) abolishes the host immune response to lipopolysaccharide (LPS), and mutation of the equivalent residue in TLR2, Pro681His, disrupts signal transduction in response to stimulation by yeast and gram-positive bacteria. Here we report the crystal structures of the TIR domains of human TLR1 and TLR2 and of the Pro681His mutant of TLR2. The structures have a large conserved surface patch that also contains the site of the Lps(d) mutation. Mutagenesis and functional studies confirm that residues in this surface patch are crucial for receptor signalling. The Lps(d) mutation does not disturb the structure of the TIR domain itself. Instead, structural and functional studies indicate that the conserved surface patch may mediate interactions with the down-stream MyD88 adapter molecule, and that the Lps(d) mutation may abolish receptor signalling by disrupting this recruitment.
-===CRYSTAL STRUCTURE OF THE TIR DOMAIN OF HUMAN TLR1===
+Structural basis for signal transduction by the Toll/interleukin-1 receptor domains.,Xu Y, Tao X, Shen B, Horng T, Medzhitov R, Manley JL, Tong L Nature. 2000 Nov 2;408(6808):111-5. PMID:11081518<ref>PMID:11081518</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1fyv" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_11081518}}, adds the Publication Abstract to the page
+*[[Toll-like Receptor 3D structures|Toll-like Receptor 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 11081518 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_11081518}}
+__TOC__
+</StructureSection>
-==About this Structure==
-FYV is a 1 chain structure of 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=1FYV OCA].
-==Reference==
-<ref group="xtra">PMID:11081518</ref><references group="xtra"/>
 [[Category: Homo sapiens]]
-[[Category: Horng, T.]]
+[[Category: Large Structures]]
-[[Category: Manley, J L.]]
+[[Category: Horng T]]
-[[Category: Medzhitov, R.]]
+[[Category: Manley JL]]
-[[Category: Shen, B.]]
+[[Category: Medzhitov R]]
-[[Category: Tao, X.]]
+[[Category: Shen B]]
-[[Category: Tong, L.]]
+[[Category: Tao X]]
-[[Category: Xu, Y.]]
+[[Category: Tong L]]
-[[Category: Beta-alpha-beta fold parallel beta sheet]]
+[[Category: Xu Y]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 11:18:48 2009''