4rt4

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
'''Unreleased structure'''
+
==Crystal structure of Dpy30 complexed with Bre2==
-
 
+
<StructureSection load='4rt4' size='340' side='right' caption='[[4rt4]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
-
The entry 4rt4 is ON HOLD until Paper Publication
+
== Structural highlights ==
-
 
+
<table><tr><td colspan='2'>[[4rt4]] is a 5 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RT4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RT4 FirstGlance]. <br>
-
Authors: Zhang, H.M., Li, M., Chang, W.R.
+
</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=4rt4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rt4 OCA], [http://pdbe.org/4rt4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rt4 RCSB], [http://www.ebi.ac.uk/pdbsum/4rt4 PDBsum]</span></td></tr>
-
 
+
</table>
-
Description: Crystal structure of Dpy30 complexed with Bre2
+
== Function ==
-
[[Category: Unreleased Structures]]
+
[[http://www.uniprot.org/uniprot/DPY30_HUMAN DPY30_HUMAN]] As part of the MLL1/MLL complex, involved in the methylation of histone H3 at 'Lys-4', particularly trimethylation. Histone H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. May play some role in histone H3 acetylation. In a teratocarcinoma cell, plays a crucial role in retinoic acid-induced differentiation along the neural lineage, regulating gene induction and H3 'Lys-4' methylation at key developmental loci. May also play an indirect or direct role in endosomal transport.<ref>PMID:19556245</ref> <ref>PMID:19651892</ref> <ref>PMID:21335234</ref> [[http://www.uniprot.org/uniprot/BRE2_YEAST BRE2_YEAST]] The COMPASS (Set1C) complex specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation.<ref>PMID:11742990</ref> <ref>PMID:11805083</ref>
-
[[Category: Zhang, H.M]]
+
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Chang, W R]]
[[Category: Li, M]]
[[Category: Li, M]]
-
[[Category: Chang, W.R]]
+
[[Category: Zhang, H M]]
 +
[[Category: H3k4 methylation]]
 +
[[Category: Protein binding]]
 +
[[Category: X-type helix]]

Revision as of 13:42, 7 October 2015

Crystal structure of Dpy30 complexed with Bre2

4rt4, resolution 2.00Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools