1kna: Difference between revisions

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[[Image:1kna.gif|left|200px]]<br /><applet load="1kna" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1kna.gif|left|200px]]<br /><applet load="1kna" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1kna, resolution 2.10Å" />

'''Chromo domain of HP1 complexed with histone H3 tail containing dimethyllysine 9.'''<br />

==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 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==

1KNA 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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1KNA OCA].

1KNA 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=1KNA OCA].

==Reference==

Line 13:

[[Category: Drosophila melanogaster]]

[[Category: Protein complex]]

[[Category: Jacobs, S.A.]]

[[Category: Jacobs, S A.]]

[[Category: Khorasanizadeh, S.]]

[[Category: chromo]]

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[[Category: methyllysine]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 19~~:23:~~43 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:35:55 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1kna.gif|left|200px]]<br /><applet load="1kna" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1kna.gif|left|200px]]<br /><applet load="1kna" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1kna, resolution 2.10&Aring;" />
 '''Chromo domain of HP1 complexed with histone H3 tail containing dimethyllysine 9.'''<br />
 ==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 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==
-KNA 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KNA OCA].
+KNA 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=1KNA OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Drosophila melanogaster]]
 [[Category: Protein complex]]
-[[Category: Jacobs, S.A.]]
+[[Category: Jacobs, S A.]]
 [[Category: Khorasanizadeh, S.]]
 [[Category: chromo]]
@@ Line 22: / Line 22: @@
 [[Category: methyllysine]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:23:43 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:35:55 2008''