2iij: Difference between revisions

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-[[Image:2iij.jpg|left|200px]]<br /><applet load="2iij" size="350" color="white" frame="true" align="right" spinBox="true"
-caption="2iij" />
-'''Structure of human Asf1a in complex with histone H3'''<br />
-==Overview==
+==Structure of human Asf1a in complex with histone H3==
+<StructureSection load='2iij' size='340' side='right'caption='[[2iij]]' scene=''>
+== Structural highlights ==
+<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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=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>
+</table>
+== Function ==
+[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>
+== 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/ii/2iij_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=2iij ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
 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.
-==About this Structure==
+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>
-IIJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=2IIJ OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17292837 17292837]
+</div>
+<div class="pdbe-citations 2iij" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Anti-silencing factor 3D structures|Anti-silencing factor 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Agez, M.]]
+[[Category: Agez M]]
-[[Category: Guerois, R.]]
+[[Category: Guerois R]]
-[[Category: Heijenoort, C van.]]
+[[Category: Mann C]]
-[[Category: Mann, C.]]
+[[Category: Ochsenbein F]]
-[[Category: Ochsenbein, F.]]
+[[Category: Van Heijenoort C]]
-[[Category: protein-protein complex]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:53:15 2008''