2h9n: Difference between revisions

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[[Image:2h9n.~~gif~~|left|200px]]

[[Image:2h9n.png|left|200px]]

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~~'''~~WDR5 in complex with monomethylated H3K4 peptide~~'''~~

===WDR5 in complex with monomethylated H3K4 peptide===

~~==Overview==~~

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~~Histone methylation at specific lysine residues brings about various downstream events that are mediated by different effector proteins.~~ The ~~WD40 domain of WDR5 represents a new class of histone methyl-lysine recognition domains that is important for recruiting H3K4 methyltransferases~~ to ~~K4-dimethylated histone H3 tail~~ as ~~well as for global and gene-specific K4 trimethylation~~. ~~Here we report the crystal structures of full-length WDR5~~, ~~WDR5Delta23 and its complexes with unmodified, mono-, di- and trimethylated histone H3K4 peptides. The structures reveal that WDR5~~ is ~~able to bind all of these histone H3 peptides, but only H3K4me2 peptide forms extra interactions with WDR5 by use of both water-mediated hydrogen bonding and~~ the ~~altered hydrophilicity of the modified lysine 4. We propose a mechanism for the involvement of WDR5 in binding and presenting histone H3K4 for further methylation as a component of MLL complexes~~.

The line below this paragraph, {{ABSTRACT_PUBMED_16946699}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 16946699 is the PubMed ID number.

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==About this Structure==

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[[Category: Structural genomics consortium]]

[[Category: Wdr5]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May 4 06~~:01:39 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 11:29:27 2008''

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-[[Image:2h9n.gif|left|200px]]
+{{Seed}}
+[[Image:2h9n.png|left|200px]]
 <!--
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 {{STRUCTURE_2h9n|  PDB=2h9n  |  SCENE=  }}
-'''WDR5 in complex with monomethylated H3K4 peptide'''
+===WDR5 in complex with monomethylated H3K4 peptide===
-==Overview==
+<!--
-Histone methylation at specific lysine residues brings about various downstream events that are mediated by different effector proteins. The WD40 domain of WDR5 represents a new class of histone methyl-lysine recognition domains that is important for recruiting H3K4 methyltransferases to K4-dimethylated histone H3 tail as well as for global and gene-specific K4 trimethylation. Here we report the crystal structures of full-length WDR5, WDR5Delta23 and its complexes with unmodified, mono-, di- and trimethylated histone H3K4 peptides. The structures reveal that WDR5 is able to bind all of these histone H3 peptides, but only H3K4me2 peptide forms extra interactions with WDR5 by use of both water-mediated hydrogen bonding and the altered hydrophilicity of the modified lysine 4. We propose a mechanism for the involvement of WDR5 in binding and presenting histone H3K4 for further methylation as a component of MLL complexes.
+The line below this paragraph, {{ABSTRACT_PUBMED_16946699}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16946699 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16946699}}
 ==About this Structure==
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 [[Category: Structural genomics consortium]]
 [[Category: Wdr5]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 06:01:39 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 11:29:27 2008''