2xl3

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (10:33, 20 December 2023) (edit) (undo)
 
(One intermediate revision not shown.)
Line 3: Line 3:
<StructureSection load='2xl3' size='340' side='right'caption='[[2xl3]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
<StructureSection load='2xl3' size='340' side='right'caption='[[2xl3]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[2xl3]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XL3 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2XL3 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[2xl3]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XL3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XL3 FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 2.7&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1u35|1u35]], [[2wp1|2wp1]], [[1guw|1guw]], [[2xl2|2xl2]]</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
-
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2xl3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xl3 OCA], [http://pdbe.org/2xl3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xl3 RCSB], [http://www.ebi.ac.uk/pdbsum/2xl3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xl3 ProSAT]</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=2xl3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xl3 OCA], [https://pdbe.org/2xl3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xl3 RCSB], [https://www.ebi.ac.uk/pdbsum/2xl3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xl3 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/WDR5_MOUSE WDR5_MOUSE]] 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 (By similarity). [[http://www.uniprot.org/uniprot/RBBP5_MOUSE RBBP5_MOUSE]] 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. 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. Does not affect ES cell self-renewal.
+
[https://www.uniprot.org/uniprot/WDR5_MOUSE WDR5_MOUSE] 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 (By similarity).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 37: Line 37:
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Lk3 transgenic mice]]
+
[[Category: Mus musculus]]
-
[[Category: Odho, Z]]
+
[[Category: Odho Z]]
-
[[Category: Southall, S M]]
+
[[Category: Southall SM]]
-
[[Category: Wilson, J R]]
+
[[Category: Wilson JR]]
-
[[Category: H3k4 methylation]]
+
-
[[Category: Mll complex]]
+
-
[[Category: Transcription]]
+
-
[[Category: Wd-40 beta-propeller]]
+

Current revision

WDR5 IN COMPLEX WITH AN RBBP5 PEPTIDE AND HISTONE H3 PEPTIDE

PDB ID 2xl3

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2xl3"
Personal tools