2i32

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{{Seed}}
 
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[[Image:2i32.png|left|200px]]
 
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==Structure of a human ASF1a-HIRA complex and insights into specificity of histone chaperone complex assembly==
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The line below this paragraph, containing "STRUCTURE_2i32", creates the "Structure Box" on the page.
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<StructureSection load='2i32' size='340' side='right'caption='[[2i32]], [[Resolution|resolution]] 2.70&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'>[[2i32]] is a 4 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=2I32 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2I32 FirstGlance]. <br>
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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]] 2.7&#8491;</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=2i32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i32 OCA], [https://pdbe.org/2i32 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2i32 RCSB], [https://www.ebi.ac.uk/pdbsum/2i32 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2i32 ProSAT]</span></td></tr>
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{{STRUCTURE_2i32| PDB=2i32 | 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/i3/2i32_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=2i32 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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Human HIRA, ASF1a, ASF1b and CAF-1 are evolutionally conserved histone chaperones that form multiple functionally distinct chromatin-assembly complexes, with roles linked to diverse nuclear process, such as DNA replication and formation of heterochromatin in senescent cells. We report the crystal structure of an ASF1a-HIRA heterodimer and a biochemical dissection of ASF1a's mutually exclusive interactions with HIRA and the p60 subunit of CAF-1. The HIRA B domain forms an antiparallel beta-hairpin that binds perpendicular to the strands of the beta-sandwich of ASF1a, via beta-sheet, salt bridge and van der Waals contacts. The N- and C-terminal regions of ASF1a and ASF1b determine the different affinities of these two proteins for HIRA, by contacting regions outside the HIRA B domain. CAF-1 p60 also uses B domain-like motifs for binding to ASF1a, thereby competing with HIRA. Together, these studies begin to define the molecular determinants of assembly of functionally diverse macromolecular histone chaperone complexes.
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===Structure of a human ASF1a-HIRA complex and insights into specificity of histone chaperone complex assembly===
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Structure of a human ASF1a-HIRA complex and insights into specificity of histone chaperone complex assembly.,Tang Y, Poustovoitov MV, Zhao K, Garfinkel M, Canutescu A, Dunbrack R, Adams PD, Marmorstein R Nat Struct Mol Biol. 2006 Oct;13(10):921-9. Epub 2006 Sep 17. PMID:16980972<ref>PMID:16980972</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 2i32" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_16980972}}, 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 16980972 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_16980972}}
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__TOC__
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</StructureSection>
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==About this Structure==
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2I32 is a 4 chains 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=2I32 OCA].
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==Reference==
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<ref group="xtra">PMID:16980972</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Marmorstein, R.]]
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[[Category: Large Structures]]
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[[Category: Tang, Y.]]
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[[Category: Marmorstein R]]
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[[Category: Asf1]]
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[[Category: Tang Y]]
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[[Category: Caf-1]]
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[[Category: Chromatin regulation]]
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[[Category: Hira]]
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[[Category: Histone chaperone]]
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[[Category: Histone deposition]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 10:09:33 2009''
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Current revision

Structure of a human ASF1a-HIRA complex and insights into specificity of histone chaperone complex assembly

PDB ID 2i32

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