2iij

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{{Seed}}
 
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[[Image:2iij.png|left|200px]]
 
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<!--
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==Structure of human Asf1a in complex with histone H3==
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The line below this paragraph, containing "STRUCTURE_2iij", creates the "Structure Box" on the page.
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<StructureSection load='2iij' size='340' side='right'caption='[[2iij]]' 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'>[[2iij]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IIJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IIJ 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">Solution NMR</td></tr>
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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=2iij FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iij OCA], [https://pdbe.org/2iij PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2iij RCSB], [https://www.ebi.ac.uk/pdbsum/2iij PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2iij ProSAT]</span></td></tr>
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{{STRUCTURE_2iij| PDB=2iij | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ASF1A_HUMAN ASF1A_HUMAN] Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly. Cooperates with chromatin assembly factor 1 (CAF-1) to promote replication-dependent chromatin assembly and with HIRA to promote replication-independent chromatin assembly. Required for the formation of senescence-associated heterochromatin foci (SAHF) and efficient senescence-associated cell cycle exit.<ref>PMID:10759893</ref> <ref>PMID:11897662</ref> <ref>PMID:12842904</ref> <ref>PMID:14718166</ref> <ref>PMID:15621527</ref> <ref>PMID:16151251</ref> <ref>PMID:15664198</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/ii/2iij_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2iij 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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Asf1 is a histone chaperone that favors histone H3/H4 assembly and disassembly. We solved the structure of the conserved domain of human ASF1A in complex with the C-terminal helix of histone H3 using nuclear magnetic resonance spectroscopy. This structure is fully compatible with an association of ASF1 with the heterodimeric form of histones H3/H4. In our model, ASF1 substitutes for the second H3/H4 heterodimer that is normally found in heterotetrameric H3/H4 complexes. This result constitutes an essential step in the fundamental understanding of the mechanisms of nucleosome assembly by histone chaperones. Point mutations that perturb the Asf1/histone interface were designed from the structure. The decreased binding affinity of the Asf1-H3/H4 complex correlates with decreased levels of H3-K56 acetylation and phenotypic defects in vivo.
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===Structure of human Asf1a in complex with histone H3===
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Structure of the histone chaperone ASF1 bound to the histone H3 C-terminal helix and functional insights.,Agez M, Chen J, Guerois R, van Heijenoort C, Thuret JY, Mann C, Ochsenbein F Structure. 2007 Feb;15(2):191-9. PMID:17292837<ref>PMID:17292837</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 2iij" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_17292837}}, adds the Publication Abstract to the page
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*[[Anti-silencing factor 3D structures|Anti-silencing factor 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 17292837 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_17292837}}
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__TOC__
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</StructureSection>
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==About this Structure==
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2IIJ is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IIJ OCA].
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==Reference==
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<ref group="xtra">PMID:17292837</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Agez, M.]]
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[[Category: Large Structures]]
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[[Category: Guerois, R.]]
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[[Category: Agez M]]
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[[Category: Heijenoort, C van.]]
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[[Category: Guerois R]]
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[[Category: Mann, C.]]
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[[Category: Mann C]]
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[[Category: Ochsenbein, F.]]
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[[Category: Ochsenbein F]]
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[[Category: Protein-protein complex]]
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[[Category: Van Heijenoort C]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 13:38:41 2009''
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Current revision

Structure of human Asf1a in complex with histone H3

PDB ID 2iij

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OCA

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