1kne
From Proteopedia
(New page: 200px<br /><applet load="1kne" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kne, resolution 2.40Å" /> '''Chromo domain of HP1...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1kne.gif|left|200px]]<br /><applet load="1kne" size=" | + | [[Image:1kne.gif|left|200px]]<br /><applet load="1kne" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1kne, resolution 2.40Å" /> | caption="1kne, resolution 2.40Å" /> | ||
'''Chromo domain of HP1 complexed with histone H3 tail containing trimethyllysine 9'''<br /> | '''Chromo domain of HP1 complexed with histone H3 tail containing trimethyllysine 9'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The chromodomain of the HP1 family of proteins recognizes histone tails | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1KNE is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http:// | + | 1KNE is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KNE OCA]. |
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Drosophila melanogaster]] | [[Category: Drosophila melanogaster]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Jacobs, S | + | [[Category: Jacobs, S A.]] |
[[Category: Khorasanizadeh, S.]] | [[Category: Khorasanizadeh, S.]] | ||
[[Category: chromatin]] | [[Category: chromatin]] | ||
| Line 23: | Line 23: | ||
[[Category: trimethyllysine]] | [[Category: trimethyllysine]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:35:59 2008'' |
Revision as of 11:35, 21 February 2008
|
Chromo domain of HP1 complexed with histone H3 tail containing trimethyllysine 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.
About this Structure
1KNE is a Protein complex structure of sequences from Drosophila melanogaster. Full crystallographic information is available from OCA.
Reference
Structure of HP1 chromodomain bound to a lysine 9-methylated histone H3 tail., Jacobs SA, Khorasanizadeh S, Science. 2002 Mar 15;295(5562):2080-3. Epub 2002 Feb 21. PMID:11859155
Page seeded by OCA on Thu Feb 21 13:35:59 2008
