1kna: Difference between revisions

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[[Image:1kna.~~gif~~|left|200px]]

[[Image:1kna.png|left|200px]]

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~~'''~~Chromo domain of HP1 complexed with histone H3 tail containing dimethyllysine 9.~~'''~~

===Chromo domain of HP1 complexed with histone H3 tail containing dimethyllysine 9.===

~~==Overview==~~

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The ~~chromodomain of the HP1 family of proteins recognizes histone tails with specifically methylated lysines. Here~~, ~~we present structural~~, ~~energetic, and mutational analyses of~~ the ~~complex between~~ the ~~Drosophila HP1 chromodomain and the histone H3 tail with a methyllysine~~ at ~~residue 9, a modification associated with epigenetic silencing~~. ~~The histone tail inserts as a beta strand~~, ~~completing the beta-sandwich architecture of the chromodomain. The methylammonium group~~ is ~~caged by three aromatic side chains, whereas adjacent residues form discerning contacts with one face of~~ the ~~chromodomain~~. ~~Comparison of dimethyl~~- ~~and trimethyllysine~~-~~containing complexes suggests a role for cation-pi and van der Waals interactions, with trimethylation slightly improving the binding affinity.~~

The line below this paragraph, {{ABSTRACT_PUBMED_11859155}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 11859155 is the PubMed ID number.

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==About this Structure==

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[[Category: Hp1]]

[[Category: Methyllysine]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ 2 22:56:31 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:35:23 2008''

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-[[Image:1kna.gif|left|200px]]
+{{Seed}}
+[[Image:1kna.png|left|200px]]
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 {{STRUCTURE_1kna|  PDB=1kna  |  SCENE=  }}
-'''Chromo domain of HP1 complexed with histone H3 tail containing dimethyllysine 9.'''
+===Chromo domain of HP1 complexed with histone H3 tail containing dimethyllysine 9.===
-==Overview==
+<!--
-The chromodomain of the HP1 family of proteins recognizes histone tails with specifically methylated lysines. Here, we present structural, energetic, and mutational analyses of the complex between the Drosophila HP1 chromodomain and the histone H3 tail with a methyllysine at residue 9, a modification associated with epigenetic silencing. The histone tail inserts as a beta strand, completing the beta-sandwich architecture of the chromodomain. The methylammonium group is caged by three aromatic side chains, whereas adjacent residues form discerning contacts with one face of the chromodomain. Comparison of dimethyl- and trimethyllysine-containing complexes suggests a role for cation-pi and van der Waals interactions, with trimethylation slightly improving the binding affinity.
+The line below this paragraph, {{ABSTRACT_PUBMED_11859155}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11859155 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11859155}}
 ==About this Structure==
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 [[Category: Hp1]]
 [[Category: Methyllysine]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 22:56:31 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul  2 10:35:23 2008''