3c99
From Proteopedia
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- | {{STRUCTURE_3c99| PDB=3c99 | SCENE= }} | ||
- | ===Structural Basis of Histone H4 Recognition by p55=== | ||
- | {{ABSTRACT_PUBMED_18443147}} | ||
- | == | + | ==Structural Basis of Histone H4 Recognition by p55== |
- | [[http://www.uniprot.org/uniprot/CAF1_DROME CAF1_DROME | + | <StructureSection load='3c99' size='340' side='right'caption='[[3c99]], [[Resolution|resolution]] 2.90Å' scene=''> |
- | + | == Structural highlights == | |
- | == | + | <table><tr><td colspan='2'>[[3c99]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C99 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3C99 FirstGlance]. <br> |
- | [[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9Å</td></tr> |
- | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></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=3c99 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c99 OCA], [https://pdbe.org/3c99 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3c99 RCSB], [https://www.ebi.ac.uk/pdbsum/3c99 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3c99 ProSAT]</span></td></tr> | |
- | < | + | </table> |
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/CAF1_DROME CAF1_DROME] Core histone-binding subunit that may target chromatin assembly factors, chromatin remodeling factors and histone deacetylases to their histone substrates in a manner that is regulated by nucleosomal DNA. Component of several complexes which regulate chromatin metabolism. These include the chromatin assembly factor 1 (CAF-1) complex, which is required for chromatin assembly following DNA replication and DNA repair; the nucleosome remodeling and deacetylase complex (the NuRD complex), which promotes transcriptional repression by histone deacetylation and nucleosome remodeling; the nucleosome remodeling factor (NURF) complex, which catalyzes ATP-dependent nucleosome sliding and facilitates transcription of chromatin; and the polycomb group (PcG) repressor complex ESC-E(Z), which promotes repression of homeotic genes during development. Also required for transcriptional repression of E2F target genes by E2f2 and Rbf or Rbf2.<ref>PMID:8887645</ref> <ref>PMID:9419341</ref> <ref>PMID:9784495</ref> <ref>PMID:12490953</ref> <ref>PMID:15456884</ref> | ||
+ | == 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/c9/3c99_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=3c99 ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
[[Category: Drosophila melanogaster]] | [[Category: Drosophila melanogaster]] | ||
- | [[Category: | + | [[Category: Large Structures]] |
- | [[Category: | + | [[Category: Garlick JD]] |
- | [[Category: | + | [[Category: Kingston RE]] |
- | [[Category: | + | [[Category: Song JJ]] |
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Current revision
Structural Basis of Histone H4 Recognition by p55
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