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| | ==Solution structure of the chromodomain of HP1a with the phosphorylated N-terminal tail complexed with H3K9me3 peptide== | | ==Solution structure of the chromodomain of HP1a with the phosphorylated N-terminal tail complexed with H3K9me3 peptide== |
| - | <StructureSection load='2rvn' size='340' side='right' caption='[[2rvn]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2rvn' size='340' side='right'caption='[[2rvn]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2rvn]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RVN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2RVN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2rvn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RVN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RVN FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=M3L:N-TRIMETHYLLYSINE'>M3L</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2rvl|2rvl]], [[2rvm|2rvm]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=M3L:N-TRIMETHYLLYSINE'>M3L</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</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=2rvn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rvn OCA], [http://pdbe.org/2rvn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2rvn RCSB], [http://www.ebi.ac.uk/pdbsum/2rvn PDBsum]</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=2rvn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rvn OCA], [https://pdbe.org/2rvn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rvn RCSB], [https://www.ebi.ac.uk/pdbsum/2rvn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rvn ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CBX5_MOUSE CBX5_MOUSE]] Component of heterochromatin that recognizes and binds histone H3 tails methylated at 'Lys-9' (H3K9me), leading to epigenetic repression. In contrast, it is excluded from chromatin when 'Tyr-41' of histone H3 is phosphorylated (H3Y41ph). Can interact with lamin-B receptor (LBR). This interaction can contribute to the association of the heterochromatin with the inner nuclear membrane. Involved in the formation of functional kinetochore through interaction with MIS12 complex proteins (By similarity). | + | [https://www.uniprot.org/uniprot/CBX5_MOUSE CBX5_MOUSE] Component of heterochromatin that recognizes and binds histone H3 tails methylated at 'Lys-9' (H3K9me), leading to epigenetic repression. In contrast, it is excluded from chromatin when 'Tyr-41' of histone H3 is phosphorylated (H3Y41ph). Can interact with lamin-B receptor (LBR). This interaction can contribute to the association of the heterochromatin with the inner nuclear membrane. Involved in the formation of functional kinetochore through interaction with MIS12 complex proteins (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Kawaguchi, A]] | + | [[Category: Large Structures]] |
| - | [[Category: Nishimura, Y]] | + | [[Category: Mus musculus]] |
| - | [[Category: Chromodomain]] | + | [[Category: Kawaguchi A]] |
| - | [[Category: Hp1alpha]] | + | [[Category: Nishimura Y]] |
| - | [[Category: Transcription-peptide complex]]
| + | |
| Structural highlights
Function
CBX5_MOUSE Component of heterochromatin that recognizes and binds histone H3 tails methylated at 'Lys-9' (H3K9me), leading to epigenetic repression. In contrast, it is excluded from chromatin when 'Tyr-41' of histone H3 is phosphorylated (H3Y41ph). Can interact with lamin-B receptor (LBR). This interaction can contribute to the association of the heterochromatin with the inner nuclear membrane. Involved in the formation of functional kinetochore through interaction with MIS12 complex proteins (By similarity).
Publication Abstract from PubMed
The chromodomain of HP1alpha binds directly to lysine 9-methylated histone H3 (H3K9me). This interaction is enhanced by phosphorylation of serine residues in the N-terminal tail of HP1alpha by unknown mechanism. Here we show that phosphorylation modulates flexibility of HP1alpha's N-terminal tail, which strengthens the interaction with H3. NMR analysis of HP1alpha's chromodomain with N-terminal tail reveals that phosphorylation does not change the overall tertiary structure, but apparently reduces the tail dynamics. Small angle X-ray scattering confirms that phosphorylation contributes to extending HP1alpha's N-terminal tail. Systematic analysis using deletion mutants and replica exchange molecular dynamics simulations indicate that the phosphorylated serines and following acidic segment behave like an extended string and dynamically bind to H3 basic residues; without phosphorylation, the most N-terminal basic segment of HP1alpha inhibits interaction of the acidic segment with H3. Thus, the dynamic string-like behavior of HP1alpha's N-terminal tail underlies the enhancement in H3 binding due to phosphorylation.
Extended string-like binding of the phosphorylated HP1alpha N-terminal tail to the lysine 9-methylated histone H3 tail.,Shimojo H, Kawaguchi A, Oda T, Hashiguchi N, Omori S, Moritsugu K, Kidera A, Hiragami-Hamada K, Nakayama J, Sato M, Nishimura Y Sci Rep. 2016 Mar 3;6:22527. doi: 10.1038/srep22527. PMID:26934956[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Shimojo H, Kawaguchi A, Oda T, Hashiguchi N, Omori S, Moritsugu K, Kidera A, Hiragami-Hamada K, Nakayama J, Sato M, Nishimura Y. Extended string-like binding of the phosphorylated HP1alpha N-terminal tail to the lysine 9-methylated histone H3 tail. Sci Rep. 2016 Mar 3;6:22527. doi: 10.1038/srep22527. PMID:26934956 doi:http://dx.doi.org/10.1038/srep22527
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