2h9m: Difference between revisions

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

OCA

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-[[Image:2h9m.gif|left|200px]]<br />
-<applet load="2h9m" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="2h9m, resolution 1.90&Aring;" />
-'''WDR5 in complex with unmodified H3K4 peptide'''<br />
-==Overview==
+==WDR5 in complex with unmodified H3K4 peptide==
-Histone methylation at specific lysine residues brings about various, downstream events that are mediated by different effector proteins. The, WD40 domain of WDR5 represents a new class of histone methyl-lysine, recognition domains that is important for recruiting H3K4, methyltransferases to K4-dimethylated histone H3 tail as well as for, global and gene-specific K4 trimethylation. Here we report the crystal, structures of full-length WDR5, WDR5Delta23 and its complexes with, unmodified, mono-, di- and trimethylated histone H3K4 peptides. The, structures reveal that WDR5 is able to bind all of these histone H3, peptides, but only H3K4me2 peptide forms extra interactions with WDR5 by, use of both water-mediated hydrogen bonding and the altered hydrophilicity, of the modified lysine 4. We propose a mechanism for the involvement of, WDR5 in binding and presenting histone H3K4 for further methylation as a, component of MLL complexes.
+<StructureSection load='2h9m' size='340' side='right'caption='[[2h9m]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2h9m]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Xenopus_tropicalis Xenopus tropicalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H9M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H9M 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]] 1.9&#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=2h9m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h9m OCA], [https://pdbe.org/2h9m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h9m RCSB], [https://www.ebi.ac.uk/pdbsum/2h9m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h9m ProSAT]</span></td></tr>
+</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/h9/2h9m_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=2h9m ConSurf].
+<div style="clear:both"></div>
-==Disease==
+==See Also==
-Known disease associated with this structure: Asphyxiating thoracic dystrophy OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=611177 611177]]
+*[[WD repeat-containing protein|WD repeat-containing protein]]
+*[[WD-repeat protein 3D structures|WD-repeat protein 3D structures]]
-==About this Structure==
+== References ==
-H9M is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=2H9M OCA].
+<references/>
+__TOC__
-==Reference==
+</StructureSection>
-Structural basis for molecular recognition and presentation of histone H3 by WDR5., Schuetz A, Allali-Hassani A, Martin F, Loppnau P, Vedadi M, Bochkarev A, Plotnikov AN, Arrowsmith CH, Min J, EMBO J. 2006 Sep 20;25(18):4245-52. Epub 2006 Aug 31. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16946699 16946699]
 [[Category: Homo sapiens]]
-[[Category: Protein complex]]
+[[Category: Large Structures]]
-[[Category: Allali-Hassani, A.]]
+[[Category: Xenopus tropicalis]]
-[[Category: Arrowsmith, C.H.]]
+[[Category: Allali-Hassani A]]
-[[Category: Bochkarev, A.]]
+[[Category: Arrowsmith CH]]
-[[Category: Edwards, A.M.]]
+[[Category: Bochkarev A]]
-[[Category: Loppnau, P.]]
+[[Category: Edwards AM]]
-[[Category: Martin, F.]]
+[[Category: Loppnau P]]
-[[Category: Min, J.R.]]
+[[Category: Martin F]]
-[[Category: Plotnikov, A.N.]]
+[[Category: Min JR]]
-[[Category: SGC, Structural.Genomics.Consortium.]]
+[[Category: Plotnikov AN]]
-[[Category: Schuetz, A.]]
+[[Category: Schuetz A]]
-[[Category: Sundstrom, M.]]
+[[Category: Sundstrom M]]
-[[Category: Vedadi, M.]]
+[[Category: Vedadi M]]
-[[Category: Weigelt, J.]]
+[[Category: Weigelt J]]
-[[Category: sgc]]
-[[Category: structural genomics]]
-[[Category: structural genomics consortium]]
-[[Category: wdr5]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:28:48 2007''