1s4z
From Proteopedia
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| - | [[Image:1s4z.gif|left|200px]]<br /><applet load="1s4z" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1s4z" /> | ||
| - | '''HP1 chromo shadow domain in complex with PXVXL motif of CAF-1'''<br /> | ||
| - | == | + | ==HP1 chromo shadow domain in complex with PXVXL motif of CAF-1== |
| + | <StructureSection load='1s4z' size='340' side='right'caption='[[1s4z]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <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='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> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [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 == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/s4/1s4z_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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="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. | 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®/PubMed®, 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__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
| - | + | [[Category: Hirshberg M]] | |
| - | [[Category: Hirshberg | + | [[Category: Laue ED]] |
| - | [[Category: Laue | + | [[Category: Lyon D]] |
| - | [[Category: Lyon | + | [[Category: Mott HR]] |
| - | [[Category: Mott | + | [[Category: Murzina NV]] |
| - | [[Category: Murzina | + | [[Category: Nielsen PR]] |
| - | [[Category: Nielsen | + | [[Category: Nietlispach D]] |
| - | [[Category: Nietlispach | + | [[Category: Okuwaki M]] |
| - | [[Category: Okuwaki | + | [[Category: Thiru A]] |
| - | [[Category: Thiru | + | [[Category: Verreault A]] |
| - | [[Category: Verreault | + | |
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
HP1 chromo shadow domain in complex with PXVXL motif of CAF-1
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Categories: Large Structures | Mus musculus | Hirshberg M | Laue ED | Lyon D | Mott HR | Murzina NV | Nielsen PR | Nietlispach D | Okuwaki M | Thiru A | Verreault A
