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==HP1 chromo shadow domain in complex with PXVXL motif of CAF-1==
==HP1 chromo shadow domain in complex with PXVXL motif of CAF-1==
<StructureSection load='1s4z' size='340' side='right'caption='[[1s4z]], [[NMR_Ensembles_of_Models | 25 NMR models]]' scene=''>
<StructureSection load='1s4z' size='340' side='right'caption='[[1s4z]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1s4z]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S4Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S4Z FirstGlance]. <br>
<table><tr><td colspan='2'>[[1s4z]] is a 3 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=1S4Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S4Z FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CBX1, CBX ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice]), CHAF1A, CAIP150 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1s4z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s4z OCA], [https://pdbe.org/1s4z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s4z RCSB], [https://www.ebi.ac.uk/pdbsum/1s4z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s4z 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=1s4z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s4z OCA], [https://pdbe.org/1s4z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s4z RCSB], [https://www.ebi.ac.uk/pdbsum/1s4z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s4z ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/CBX1_HUMAN CBX1_HUMAN]] Component of heterochromatin. Recognizes and binds histone H3 tails methylated at 'Lys-9', leading to epigenetic repression. Interaction with lamin B receptor (LBR) can contribute to the association of the heterochromatin with the inner nuclear membrane. [[https://www.uniprot.org/uniprot/CAF1A_MOUSE CAF1A_MOUSE]] Core component of the CAF-1 complex, a complex thought to mediate chromatin assembly in DNA replication and DNA repair. Assembles histone octamers onto replicating DNA in vitro. CAF-1 performs the first step of the nucleosome assembly process, bringing newly synthesized histones H3 and H4 to replicating DNA; histones H2A/H2B can bind to this chromatin precursor subsequent to DNA replication to complete the histone octamer. CHAF1A binds to histones H3 and H4. It may play a role in heterochromatin maintenance in proliferating cells by bringing newly synthesized cbx proteins to heterochromatic DNA replication foci. The CCR4-NOT complex functions as general transcription regulation complex. Also involved in vitamin D-coupled transcription regulation via its association with the WINAC complex, a chromatin-remodeling complex recruited by vitamin D receptor (VDR), which is required for the ligand-bound VDR-mediated transrepression of the CYP27B1 gene (By similarity).  
[https://www.uniprot.org/uniprot/CBX1_MOUSE CBX1_MOUSE] Component of heterochromatin. Recognizes and binds histone H3 tails methylated at 'Lys-9', leading to epigenetic repression. Interaction with lamin B receptor (LBR) can contribute to the association of the heterochromatin with the inner nuclear membrane.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1s4z ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1s4z ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
HP1 family proteins are adaptor molecules, containing two related chromo domains that are required for chromatin packaging and gene silencing. Here we present the structure of the chromo shadow domain from mouse HP1beta bound to a peptide containing a consensus PXVXL motif found in many HP1 binding partners. The shadow domain exhibits a novel mode of peptide recognition, where the peptide binds across the dimer interface, sandwiched in a beta-sheet between strands from each monomer. The structure allows us to predict which other shadow domains bind similar PXVXL motif-containing peptides and provides a framework for predicting the sequence specificity of the others. We show that targeting of HP1beta to heterochromatin requires shadow domain interactions with PXVXL-containing proteins in addition to chromo domain recognition of Lys-9-methylated histone H3. Interestingly, it also appears to require the simultaneous recognition of two Lys-9-methylated histone H3 molecules. This finding implies a further complexity to the histone code for regulation of chromatin structure and suggests how binding of HP1 family proteins may lead to its condensation.
Structural basis of HP1/PXVXL motif peptide interactions and HP1 localisation to heterochromatin.,Thiru A, Nietlispach D, Mott HR, Okuwaki M, Lyon D, Nielsen PR, Hirshberg M, Verreault A, Murzina NV, Laue ED EMBO J. 2004 Feb 11;23(3):489-99. Epub 2004 Feb 5. PMID:14765118<ref>PMID:14765118</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1s4z" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Lk3 transgenic mice]]
[[Category: Mus musculus]]
[[Category: Hirshberg, M]]
[[Category: Hirshberg M]]
[[Category: Laue, E D]]
[[Category: Laue ED]]
[[Category: Lyon, D]]
[[Category: Lyon D]]
[[Category: Mott, H R]]
[[Category: Mott HR]]
[[Category: Murzina, N V]]
[[Category: Murzina NV]]
[[Category: Nielsen, P R]]
[[Category: Nielsen PR]]
[[Category: Nietlispach, D]]
[[Category: Nietlispach D]]
[[Category: Okuwaki, M]]
[[Category: Okuwaki M]]
[[Category: Thiru, A]]
[[Category: Thiru A]]
[[Category: Verreault, A]]
[[Category: Verreault A]]
[[Category: Gene regulation]]

Revision as of 11:29, 1 May 2024

HP1 chromo shadow domain in complex with PXVXL motif of CAF-1HP1 chromo shadow domain in complex with PXVXL motif of CAF-1

Structural highlights

1s4z is a 3 chain structure with sequence from Mus musculus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CBX1_MOUSE Component of heterochromatin. Recognizes and binds histone H3 tails methylated at 'Lys-9', leading to epigenetic repression. Interaction with lamin B receptor (LBR) can contribute to the association of the heterochromatin with the inner nuclear membrane.

Evolutionary Conservation

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

Drag the structure with the mouse to rotate

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