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==STRUCTURE OF THE CHROMATIN BINDING (CHROMO) DOMAIN FROM MOUSE MODIFIER PROTEIN 1, NMR, 26 STRUCTURES== | ==STRUCTURE OF THE CHROMATIN BINDING (CHROMO) DOMAIN FROM MOUSE MODIFIER PROTEIN 1, NMR, 26 STRUCTURES== | ||
<StructureSection load='1ap0' size='340' side='right' caption='[[1ap0 | <StructureSection load='1ap0' size='340' side='right'caption='[[1ap0]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ap0]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1ap0]] is a 1 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=1AP0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AP0 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | ||
<table> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ap0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ap0 OCA], [https://pdbe.org/1ap0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ap0 RCSB], [https://www.ebi.ac.uk/pdbsum/1ap0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ap0 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ap/1ap0_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ap/1ap0_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | </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=1ap0 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
| Line 23: | Line 27: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1ap0" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Archer | [[Category: Archer SJ]] | ||
[[Category: Ball | [[Category: Ball LJ]] | ||
[[Category: Broadhurst | [[Category: Broadhurst RW]] | ||
[[Category: Domaille | [[Category: Domaille PJ]] | ||
[[Category: Laue | [[Category: Laue ED]] | ||
[[Category: Murzin | [[Category: Murzin AG]] | ||
[[Category: Murzina | [[Category: Murzina NV]] | ||
[[Category: Raine | [[Category: Raine ARC]] | ||
[[Category: Singh | [[Category: Singh PB]] | ||
[[Category: Stott | [[Category: Stott FJ]] | ||
Latest revision as of 11:14, 22 May 2024
STRUCTURE OF THE CHROMATIN BINDING (CHROMO) DOMAIN FROM MOUSE MODIFIER PROTEIN 1, NMR, 26 STRUCTURESSTRUCTURE OF THE CHROMATIN BINDING (CHROMO) DOMAIN FROM MOUSE MODIFIER PROTEIN 1, NMR, 26 STRUCTURES
Structural highlights
FunctionCBX1_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. Publication Abstract from PubMedThe structure of a chromatin binding domain from mouse chromatin modifier protein 1 (MoMOD1) was determined using nuclear magnetic resonance (NMR) spectroscopy. The protein consists of an N-terminal three-stranded anti-parallel beta-sheet which folds against a C-terminal alpha-helix. The structure reveals an unexpected homology to two archaebacterial DNA binding proteins which are also involved in chromatin structure. Structural comparisons suggest that chromo domains, of which more than 40 are now known, act as protein interaction motifs and that the MoMOD1 protein acts as an adaptor mediating interactions between different proteins. Structure of the chromatin binding (chromo) domain from mouse modifier protein 1.,Ball LJ, Murzina NV, Broadhurst RW, Raine AR, Archer SJ, Stott FJ, Murzin AG, Singh PB, Domaille PJ, Laue ED EMBO J. 1997 May 1;16(9):2473-81. PMID:9171360[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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