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.


3n0e

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:3n0e.png|left|200px]]
 
- 
-
<!--
 
-
The line below this paragraph, containing "STRUCTURE_3n0e", creates the "Structure Box" on the page.
 
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
 
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
 
-
or leave the SCENE parameter empty for the default display.
 
-
-->
 
{{STRUCTURE_3n0e| PDB=3n0e | SCENE= }}
{{STRUCTURE_3n0e| PDB=3n0e | SCENE= }}
- 
===Crystal structure of WDR5 mutant (W330Y)===
===Crystal structure of WDR5 mutant (W330Y)===
 +
{{ABSTRACT_PUBMED_20939513}}
-
 
+
==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>
-
The line below this paragraph, {{ABSTRACT_PUBMED_20939513}}, adds the Publication Abstract to the page
+
-
(as it appears on PubMed at http://www.pubmed.gov), where 20939513 is the PubMed ID number.
+
-
-->
+
-
{{ABSTRACT_PUBMED_20939513}}
+
==About this Structure==
==About this Structure==
-
3N0E is a 1 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=3N0E OCA].
+
[[3n0e]] is a 1 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=3N0E OCA].
==Reference==
==Reference==
-
<ref group="xtra">PMID:20939513</ref><references group="xtra"/>
+
<ref group="xtra">PMID:020939513</ref><references group="xtra"/><references/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Chen, R C.]]
[[Category: Chen, R C.]]
Line 37: Line 24:
[[Category: Wd-repeat protein 5]]
[[Category: Wd-repeat protein 5]]
[[Category: Wdr5]]
[[Category: Wdr5]]
- 
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 1 11:01:17 2010''
 

Revision as of 20:48, 17 April 2013

Template:STRUCTURE 3n0e

Contents

Crystal structure of WDR5 mutant (W330Y)

Template:ABSTRACT PUBMED 20939513

Function

[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.[1] [2] [3] [4] [5]

About this Structure

3n0e is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

  • Wu XH, Chen RC, Gao Y, Wu YD. The Effect of Asp-His-Ser/Thr-Trp Tetrad on the Thermostability of WD40-Repeat Proteins. Biochemistry. 2010 Nov 30;49(47):10237-45. Epub 2010 Nov 8. PMID:20939513 doi:10.1021/bi101321y
  1. ↑ Patel A, Dharmarajan V, Vought VE, Cosgrove MS. On the mechanism of multiple lysine methylation by the human mixed lineage leukemia protein-1 (MLL1) core complex. J Biol Chem. 2009 Sep 4;284(36):24242-56. Epub 2009 Jun 25. PMID:19556245 doi:M109.014498
  2. ↑ Guelman S, Kozuka K, Mao Y, Pham V, Solloway MJ, Wang J, Wu J, Lill JR, Zha J. The double-histone-acetyltransferase complex ATAC is essential for mammalian development. Mol Cell Biol. 2009 Mar;29(5):1176-88. doi: 10.1128/MCB.01599-08. Epub 2008 Dec, 22. PMID:19103755 doi:10.1128/MCB.01599-08
  3. ↑ Cai Y, Jin J, Swanson SK, Cole MD, Choi SH, Florens L, Washburn MP, Conaway JW, Conaway RC. Subunit composition and substrate specificity of a MOF-containing histone acetyltransferase distinct from the male-specific lethal (MSL) complex. J Biol Chem. 2010 Feb 12;285(7):4268-72. doi: 10.1074/jbc.C109.087981. Epub 2009 , Dec 14. PMID:20018852 doi:10.1074/jbc.C109.087981
  4. ↑ Han Z, Guo L, Wang H, Shen Y, Deng XW, Chai J. Structural basis for the specific recognition of methylated histone H3 lysine 4 by the WD-40 protein WDR5. Mol Cell. 2006 Apr 7;22(1):137-44. PMID:16600877 doi:10.1016/j.molcel.2006.03.018
  5. ↑ Couture JF, Collazo E, Trievel RC. Molecular recognition of histone H3 by the WD40 protein WDR5. Nat Struct Mol Biol. 2006 Aug;13(8):698-703. Epub 2006 Jul 9. PMID:16829960 doi:10.1038/nsmb1116

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3n0e"
Personal tools