2h13: Difference between revisions

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[[Image:2h13.~~gif~~|left|200px]]

[[Image:2h13.png|left|200px]]

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~~'''~~Crystal structure of WDR5/histone H3 complex~~'''~~

===Crystal structure of WDR5/histone H3 complex===

~~==Overview==~~

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The WD40-repeat protein WDR5 is a conserved subunit of Trithorax (TRX) histone methyltransferase complexes. WDR5 has been reported to selectively bind dimethylated Lys4 (K4me2) in histone H3 to promote K4 trimethylation by TRX. To elucidate the basis of this ~~binding specificity~~, ~~we have determined~~ the ~~crystal structure of WDR5 bound~~ to ~~a histone H3 peptide bearing K4me2. The structure reveals that~~ the ~~N terminus of histone H3 binds~~ as ~~a 3(10~~)~~-helix in the central depression formed by the WD40 repeats. R2 in histone H3~~ is ~~bound in~~ the ~~acidic channel in the protein's core, whereas K4me2 is solvent exposed and does not engage in direct interactions with WDR5~~. ~~Functional studies confirm that WDR5 recognizes A1, R2 and T3 in histone H3 but has virtually identical affinities for the unmodified and mono~~-~~, di~~- ~~and trimethylated forms of K4, demonstrating that it does not discriminate among different degrees of methylation of this residue.~~

The line below this paragraph, {{ABSTRACT_PUBMED_16829960}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 16829960 is the PubMed ID number.

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==About this Structure==

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[[Category: Mll]]

[[Category: Wd40-repeat]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May 4~~ 05:44:38 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 05:29:21 2008''

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-[[Image:2h13.gif|left|200px]]
+{{Seed}}
+[[Image:2h13.png|left|200px]]
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 {{STRUCTURE_2h13|  PDB=2h13  |  SCENE=  }}
-'''Crystal structure of WDR5/histone H3 complex'''
+===Crystal structure of WDR5/histone H3 complex===
-==Overview==
+<!--
-The WD40-repeat protein WDR5 is a conserved subunit of Trithorax (TRX) histone methyltransferase complexes. WDR5 has been reported to selectively bind dimethylated Lys4 (K4me2) in histone H3 to promote K4 trimethylation by TRX. To elucidate the basis of this binding specificity, we have determined the crystal structure of WDR5 bound to a histone H3 peptide bearing K4me2. The structure reveals that the N terminus of histone H3 binds as a 3(10)-helix in the central depression formed by the WD40 repeats. R2 in histone H3 is bound in the acidic channel in the protein's core, whereas K4me2 is solvent exposed and does not engage in direct interactions with WDR5. Functional studies confirm that WDR5 recognizes A1, R2 and T3 in histone H3 but has virtually identical affinities for the unmodified and mono-, di- and trimethylated forms of K4, demonstrating that it does not discriminate among different degrees of methylation of this residue.
+The line below this paragraph, {{ABSTRACT_PUBMED_16829960}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16829960 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16829960}}
 ==About this Structure==
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 [[Category: Mll]]
 [[Category: Wd40-repeat]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 05:44:38 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 05:29:21 2008''