3cfs

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{{Seed}}
 
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[[Image:3cfs.png|left|200px]]
 
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==Structural basis of the interaction of RbAp46/RbAp48 with histone H4==
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The line below this paragraph, containing "STRUCTURE_3cfs", creates the "Structure Box" on the page.
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<StructureSection load='3cfs' size='340' side='right'caption='[[3cfs]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3cfs]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CFS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CFS FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ARS:ARSENIC'>ARS</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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{{STRUCTURE_3cfs| PDB=3cfs | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3cfs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cfs OCA], [https://pdbe.org/3cfs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cfs RCSB], [https://www.ebi.ac.uk/pdbsum/3cfs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cfs ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RBBP7_HUMAN RBBP7_HUMAN] Core histone-binding subunit that may target chromatin remodeling factors, histone acetyltransferases 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 type B histone acetyltransferase (HAT) complex, which is required for chromatin assembly following DNA replication; 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; and the PRC2/EED-EZH2 complex, which promotes repression of homeotic genes during development; and the NURF (nucleosome remodeling factor) complex.<ref>PMID:10866654</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cf/3cfs_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=3cfs ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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RbAp46 and RbAp48 (pRB-associated proteins p46 and p48, also known as RBBP7 and RBBP4, respectively) are highly homologous histone chaperones that play key roles in establishing and maintaining chromatin structure. We report here the crystal structure of human RbAp46 bound to histone H4. RbAp46 folds into a seven-bladed beta propeller structure and binds histone H4 in a groove formed between an N-terminal alpha helix and an extended loop inserted into blade six. Surprisingly, histone H4 adopts a different conformation when interacting with RbAp46 than it does in either the nucleosome or in the complex with ASF1, another histone chaperone. Our structural and biochemical results suggest that when a histone H3/H4 dimer (or tetramer) binds to RbAp46 or RbAp48, helix 1 of histone H4 unfolds to interact with the histone chaperone. We discuss the implications of our findings for the assembly and function of RbAp46 and RbAp48 complexes.
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===Structural basis of the interaction of RbAp46/RbAp48 with histone H4===
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Structural basis for the recognition of histone H4 by the histone-chaperone RbAp46.,Murzina NV, Pei XY, Zhang W, Sparkes M, Vicente-Garcia J, Pratap JV, McLaughlin SH, Ben-Shahar TR, Verreault A, Luisi BF, Laue ED Structure. 2008 Jul;16(7):1077-85. Epub 2008 Jun 19. PMID:18571423<ref>PMID:18571423</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3cfs" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_18571423}}, adds the Publication Abstract to the page
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*[[Retinoblastoma-binding protein|Retinoblastoma-binding protein]]
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(as it appears on PubMed at http://www.pubmed.gov), where 18571423 is the PubMed ID number.
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*[[Retinoblastoma-binding protein 3D structures|Retinoblastoma-binding protein 3D structures]]
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== References ==
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{{ABSTRACT_PUBMED_18571423}}
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<references/>
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__TOC__
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==About this Structure==
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</StructureSection>
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3CFS is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CFS OCA].
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==Reference==
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Structural Basis for the Recognition of Histone H4 by the Histone-Chaperone RbAp46., Murzina NV, Pei XY, Zhang W, Sparkes M, Vicente-Garcia J, Pratap JV, McLaughlin SH, Ben-Shahar TR, Verreault A, Luisi BF, Laue ED, Structure. 2008 Jul;16(7):1077-85. Epub 2008 Jun 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18571423 18571423]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Ben-Shahar, T R.]]
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[[Category: Ben-Shahar TR]]
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[[Category: Laue, E D.]]
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[[Category: Laue ED]]
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[[Category: Luisi, B F.]]
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[[Category: Luisi BF]]
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[[Category: Murzina, N V.]]
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[[Category: Murzina NV]]
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[[Category: Pei, X-Y.]]
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[[Category: Pei X-Y]]
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[[Category: Pratap, J V.]]
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[[Category: Pratap JV]]
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[[Category: Sparkes, M.]]
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[[Category: Sparkes M]]
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[[Category: Verreault, A.]]
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[[Category: Verreault A]]
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[[Category: Vicente-Garcia, J.]]
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[[Category: Vicente-Garcia J]]
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[[Category: Acetylation]]
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[[Category: Chaperone]]
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[[Category: Chromatin]]
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[[Category: Chromatin regulator]]
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[[Category: Chromosomal protein]]
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[[Category: Dna replication]]
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[[Category: Histone]]
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[[Category: Histone/chaperone complex]]
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[[Category: Nucleosome core]]
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[[Category: Nucleus]]
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[[Category: Phosphoprotein]]
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[[Category: Rbap46/rbap48]]
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[[Category: Repressor]]
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[[Category: Transcription]]
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[[Category: Transcription regulation]]
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[[Category: Wd repeat]]
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[[Category: Wd-40 repeat protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 16 08:48:29 2008''
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Current revision

Structural basis of the interaction of RbAp46/RbAp48 with histone H4

PDB ID 3cfs

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