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5y1u
From Proteopedia
(Difference between revisions)
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==Crystal structure of RBBP4 bound to AEBP2 RRK motif== | ==Crystal structure of RBBP4 bound to AEBP2 RRK motif== | ||
| - | <StructureSection load='5y1u' size='340' side='right' caption='[[5y1u]], [[Resolution|resolution]] 2.14Å' scene=''> | + | <StructureSection load='5y1u' size='340' side='right'caption='[[5y1u]], [[Resolution|resolution]] 2.14Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5y1u]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y1U OCA]. For a <b>guided tour on the structure components</b> use [http:// | + | <table><tr><td colspan='2'>[[5y1u]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y1U OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5Y1U FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5y1u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y1u OCA], [http://pdbe.org/5y1u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5y1u RCSB], [http://www.ebi.ac.uk/pdbsum/5y1u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5y1u ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/RBBP4_HUMAN RBBP4_HUMAN]] 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 core histone deacetylase (HDAC) complex, which promotes histone deacetylation and consequent transcriptional repression; the nucleosome remodeling and histone deacetylase complex (the NuRD complex), which promotes transcriptional repression by histone deacetylation and nucleosome remodeling; the PRC2/EED-EZH2 complex, which promotes repression of homeotic genes during development; and the NURF (nucleosome remodeling factor) complex.<ref>PMID:10866654</ref> [[http://www.uniprot.org/uniprot/AEBP2_HUMAN AEBP2_HUMAN]] DNA-binding transcriptional repressor. May interact with and stimulate the activity of the PRC2 complex, which methylates 'Lys-9' and 'Lys-27' residues of histone H3.<ref>PMID:15225548</ref> | [[http://www.uniprot.org/uniprot/RBBP4_HUMAN RBBP4_HUMAN]] 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 core histone deacetylase (HDAC) complex, which promotes histone deacetylation and consequent transcriptional repression; the nucleosome remodeling and histone deacetylase complex (the NuRD complex), which promotes transcriptional repression by histone deacetylation and nucleosome remodeling; the PRC2/EED-EZH2 complex, which promotes repression of homeotic genes during development; and the NURF (nucleosome remodeling factor) complex.<ref>PMID:10866654</ref> [[http://www.uniprot.org/uniprot/AEBP2_HUMAN AEBP2_HUMAN]] DNA-binding transcriptional repressor. May interact with and stimulate the activity of the PRC2 complex, which methylates 'Lys-9' and 'Lys-27' residues of histone H3.<ref>PMID:15225548</ref> | ||
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| + | ==See Also== | ||
| + | *[[Retinoblastoma-binding protein 3D structures|Retinoblastoma-binding protein 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Li, F]] | [[Category: Li, F]] | ||
[[Category: Shi, Y]] | [[Category: Shi, Y]] | ||
Revision as of 07:03, 14 October 2020
Crystal structure of RBBP4 bound to AEBP2 RRK motif
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Categories: Large Structures | Li, F | Shi, Y | Sun, A | Wu, J | Aebp2 | Gene regulation | Rbap48 | Rbbp4 | Wd40
