This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


4x8n

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (21:18, 12 April 2023) (edit) (undo)
 
(3 intermediate revisions not shown.)
Line 1: Line 1:
 +
==Crystal structure of Ash2L SPRY domain in complex with phosphorylated RbBP5==
==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 ==
== 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='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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4x8p|4x8p]]</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>
-
<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>
+
</table>
</table>
== Function ==
== 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;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 17: Line 17:
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
 +
<div class="pdbe-citations 4x8n" style="background-color:#fffaf0;"></div>
 +
 +
==See Also==
 +
*[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</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]]
+

Current revision

Crystal structure of Ash2L SPRY domain in complex with phosphorylated RbBP5

PDB ID 4x8n

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/4x8n"
Personal tools