1kna

From Proteopedia

(Difference between revisions)

Revision as of 08:49, 21 April 2021

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

Structural highlights

1kna is a 2 chain structure with sequence from Drome. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[HP1_DROME] Structural component of heterochromatin, involved in gene repression and the modification of position-effect-variegation. Recognizes and binds histone H3 tails methylated at 'Lys-9', leading to epigenetic repression.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Jacobs SA, Khorasanizadeh S. Structure of HP1 chromodomain bound to a lysine 9-methylated histone H3 tail. Science. 2002 Mar 15;295(5562):2080-3. Epub 2002 Feb 21. PMID:11859155 doi:10.1126/science.1069473

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1kna"

@@ Line 3: / Line 3: @@
 <StructureSection load='1kna' size='340' side='right'caption='[[1kna]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1kna]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KNA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KNA FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1kna]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KNA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KNA FirstGlance]. <br>
 </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kna FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kna OCA], [http://pdbe.org/1kna PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kna RCSB], [http://www.ebi.ac.uk/pdbsum/1kna PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1kna ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1kna FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kna OCA], [https://pdbe.org/1kna PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kna RCSB], [https://www.ebi.ac.uk/pdbsum/1kna PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kna ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/HP1_DROME HP1_DROME]] Structural component of heterochromatin, involved in gene repression and the modification of position-effect-variegation. Recognizes and binds histone H3 tails methylated at 'Lys-9', leading to epigenetic repression.
+[[https://www.uniprot.org/uniprot/HP1_DROME HP1_DROME]] Structural component of heterochromatin, involved in gene repression and the modification of position-effect-variegation. Recognizes and binds histone H3 tails methylated at 'Lys-9', leading to epigenetic repression.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1kna

From Proteopedia

Revision as of 08:49, 21 April 2021

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox