2h14: Difference between revisions

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-[[Image:2h14.gif|left|200px]]
-<!--
+==Crystal of WDR5 (apo-form)==
-The line below this paragraph, containing "STRUCTURE_2h14", creates the "Structure Box" on the page.
+<StructureSection load='2h14' size='340' side='right'caption='[[2h14]], [[Resolution|resolution]] 1.48&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'>[[2h14]] 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=2H14 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H14 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]] 1.48&#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=2h14 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h14 OCA], [https://pdbe.org/2h14 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h14 RCSB], [https://www.ebi.ac.uk/pdbsum/2h14 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h14 ProSAT]</span></td></tr>
-{{STRUCTURE_2h14|  PDB=2h14  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/WDR5_HUMAN WDR5_HUMAN] Contributes to histone modification. May position the N-terminus of histone H3 for efficient trimethylation at 'Lys-4'. As part of the MLL1/MLL complex it is involved in methylation and dimethylation at 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. May regulate osteoblasts differentiation.<ref>PMID:19556245</ref> <ref>PMID:19103755</ref> <ref>PMID:20018852</ref> <ref>PMID:16600877</ref> <ref>PMID:16829960</ref>
+== 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/h1/2h14_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=2h14 ConSurf].
+<div style="clear:both"></div>
-'''Crystal of WDR5 (apo-form)'''
+==See Also==
+*[[WD-repeat protein 3D structures|WD-repeat protein 3D structures]]
+== References ==
-==Overview==
+<references/>
-The WD40-repeat protein WDR5 is a conserved subunit of Trithorax (TRX) histone methyltransferase complexes. WDR5 has been reported to selectively bind dimethylated Lys4 (K4me2) in histone H3 to promote K4 trimethylation by TRX. To elucidate the basis of this binding specificity, we have determined the crystal structure of WDR5 bound to a histone H3 peptide bearing K4me2. The structure reveals that the N terminus of histone H3 binds as a 3(10)-helix in the central depression formed by the WD40 repeats. R2 in histone H3 is bound in the acidic channel in the protein's core, whereas K4me2 is solvent exposed and does not engage in direct interactions with WDR5. Functional studies confirm that WDR5 recognizes A1, R2 and T3 in histone H3 but has virtually identical affinities for the unmodified and mono-, di- and trimethylated forms of K4, demonstrating that it does not discriminate among different degrees of methylation of this residue.
+__TOC__
+</StructureSection>
-==About this Structure==
-H14 is a [[Single protein]] 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=2H14 OCA].
-==Reference==
-Molecular recognition of histone H3 by the WD40 protein WDR5., Couture JF, Collazo E, Trievel RC, Nat Struct Mol Biol. 2006 Aug;13(8):698-703. Epub 2006 Jul 9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16829960 16829960]
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Collazo, E.]]
+[[Category: Collazo E]]
-[[Category: Couture, J F.]]
+[[Category: Couture JF]]
-[[Category: Trievel, R C.]]
+[[Category: Trievel RC]]
-[[Category: Beta-propeller]]
-[[Category: Histone]]
-[[Category: Mll]]
-[[Category: Wd-40 repeat]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 05:44:39 2008''