4x8n: Difference between revisions

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 ==Crystal structure of Ash2L SPRY domain in complex with phosphorylated RbBP5==
-<StructureSection load='4x8n' size='340' side='right' caption='[[4x8n]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
+<StructureSection load='4x8n' size='340' side='right'caption='[[4x8n]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4x8n]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X8N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4X8N FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4x8n]] 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=4X8N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4X8N FirstGlance]. <br>
-</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></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]] 2.1&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4x8p|4x8p]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></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=4x8n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x8n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4x8n RCSB], [http://www.ebi.ac.uk/pdbsum/4x8n PDBsum]</span></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=4x8n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x8n OCA], [https://pdbe.org/4x8n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4x8n RCSB], [https://www.ebi.ac.uk/pdbsum/4x8n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4x8n ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/ASH2L_HUMAN ASH2L_HUMAN]] Component of the Set1/Ash2 histone methyltransferase (HMT) complex, a complex that specifically methylates 'Lys-4' of histone H3, but not if the neighboring 'Lys-9' residue is already methylated. As part of the MLL1/MLL complex it is involved in methylation and dimethylation at 'Lys-4' of histone H3. May function as a transcriptional regulator. May play a role in hematopoiesis.<ref>PMID:12670868</ref> <ref>PMID:19556245</ref>  [[http://www.uniprot.org/uniprot/RBBP5_HUMAN RBBP5_HUMAN]] In embryonic stem (ES) cells, plays a crucial role in the differentiation potential, particularly along the neural lineage, regulating gene induction and H3 'Lys-4' methylation at key developmental loci, including that mediated by retinoic acid (By similarity). As part of the MLL1/MLL complex, involved in mono-, di- and trimethylation at 'Lys-4' of histone H3. Histone H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation.<ref>PMID:19556245</ref>
+[https://www.uniprot.org/uniprot/ASH2L_HUMAN ASH2L_HUMAN] Component of the Set1/Ash2 histone methyltransferase (HMT) complex, a complex that specifically methylates 'Lys-4' of histone H3, but not if the neighboring 'Lys-9' residue is already methylated. As part of the MLL1/MLL complex it is involved in methylation and dimethylation at 'Lys-4' of histone H3. May function as a transcriptional regulator. May play a role in hematopoiesis.<ref>PMID:12670868</ref> <ref>PMID:19556245</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 17: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4x8n" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Brand, M]]
+[[Category: Homo sapiens]]
-[[Category: Brunzelle, J S]]
+[[Category: Large Structures]]
-[[Category: Chaturvedi, C P]]
+[[Category: Brand M]]
-[[Category: Couture, J F]]
+[[Category: Brunzelle JS]]
-[[Category: Shilatifard, A]]
+[[Category: Chaturvedi CP]]
-[[Category: Skiniotis, G]]
+[[Category: Couture J-F]]
-[[Category: Zhang, P]]
+[[Category: Shilatifard A]]
-[[Category: Chromatin]]
+[[Category: Skiniotis G]]
-[[Category: Epigenetic]]
+[[Category: Zhang P]]
-[[Category: Histone]]
-[[Category: Mll1]]
-[[Category: Protein binding]]