4es0: Difference between revisions

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 ==X-ray structure of WDR5-SETd1b Win motif peptide binary complex==
-<StructureSection load='4es0' size='340' side='right' caption='[[4es0]], [[Resolution|resolution]] 1.82&Aring;' scene=''>
+<StructureSection load='4es0' size='340' side='right'caption='[[4es0]], [[Resolution|resolution]] 1.82&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4es0]] is a 2 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=4ES0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ES0 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4es0]] is a 2 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=4ES0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ES0 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4erq|4erq]], [[4ery|4ery]], [[4erz|4erz]], [[4esg|4esg]]</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.817&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BIG3, WDR5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=4es0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4es0 OCA], [https://pdbe.org/4es0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4es0 RCSB], [https://www.ebi.ac.uk/pdbsum/4es0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4es0 ProSAT]</span></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone-lysine_N-methyltransferase Histone-lysine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.43 2.1.1.43] </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=4es0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4es0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4es0 RCSB], [http://www.ebi.ac.uk/pdbsum/4es0 PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://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>  [[http://www.uniprot.org/uniprot/SET1B_HUMAN SET1B_HUMAN]] Histone methyltransferase that specifically methylates 'Lys-4' of histone H3, when part of the SET1 histone methyltransferase (HMT) complex, but not if the neighboring 'Lys-9' residue is already methylated. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. The non-overalpping localization with SETD1A suggests that SETD1A and SETD1B make non-redundant contributions to the epigenetic control of chromatin structure and gene expression. Specifically tri-methylates 'Lys-4' of histone H3 in vitro.
+[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>
+==See Also==
+*[[WD-repeat protein 3D structures|WD-repeat protein 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Histone-lysine N-methyltransferase]]
 [[Category: Homo sapiens]]
-[[Category: Cosgrove, M S]]
+[[Category: Large Structures]]
-[[Category: Dharmarajan, V]]
+[[Category: Cosgrove MS]]
-[[Category: Lee, J H]]
+[[Category: Dharmarajan V]]
-[[Category: Patel, A]]
+[[Category: Lee J-H]]
-[[Category: Skalnik, D G]]
+[[Category: Patel A]]
-[[Category: 3-10 helix]]
+[[Category: Skalnik DG]]
-[[Category: Ash2l]]
-[[Category: Beta propeller]]
-[[Category: Core complex]]
-[[Category: Histone]]
-[[Category: Lysine methyltransferase]]
-[[Category: Mll1]]
-[[Category: Rbbp5]]
-[[Category: Setd1b]]
-[[Category: Transcription-transferase complex]]
-[[Category: Wd40]]
-[[Category: Win motif]]