1tey

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{{Seed}}
 
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[[Image:1tey.png|left|200px]]
 
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==NMR structure of human histone chaperone, ASF1A==
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The line below this paragraph, containing "STRUCTURE_1tey", creates the "Structure Box" on the page.
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<StructureSection load='1tey' size='340' side='right'caption='[[1tey]]' 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'>[[1tey]] is a 1 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=1TEY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TEY 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=1tey FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tey OCA], [https://pdbe.org/1tey PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tey RCSB], [https://www.ebi.ac.uk/pdbsum/1tey PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tey ProSAT]</span></td></tr>
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{{STRUCTURE_1tey| PDB=1tey | 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/te/1tey_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=1tey 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 conserved histone chaperone implicated in nucleosome assembly, transcriptional silencing, and the cellular response to DNA damage. We solved the NMR solution structure of the N-terminal functional domain of the human Asf1a isoform, and we identified by NMR chemical shift mapping a surface of Asf1a that binds the C-terminal helix of histone H3. This binding surface forms a highly conserved hydrophobic groove surrounded by charged residues. Mutations within this binding site decreased the affinity of Asf1a for the histone H3/H4 complex in vitro, and the same mutations in the homologous yeast protein led to transcriptional silencing defects, DNA damage sensitivity, and thermosensitive growth. We have thus obtained direct experimental evidence of the mode of binding between a histone and one of its chaperones and genetic data suggesting that this interaction is important in both the DNA damage response and transcriptional silencing.
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===NMR structure of human histone chaperone, ASF1A===
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Structural basis for the interaction of Asf1 with histone H3 and its functional implications.,Mousson F, Lautrette A, Thuret JY, Agez M, Courbeyrette R, Amigues B, Becker E, Neumann JM, Guerois R, Mann C, Ochsenbein F Proc Natl Acad Sci U S A. 2005 Apr 26;102(17):5975-80. Epub 2005 Apr 19. PMID:15840725<ref>PMID:15840725</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 1tey" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_15840725}}, 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 15840725 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_15840725}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1TEY is a 1 chain structure of sequence 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=1TEY OCA].
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==Reference==
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<ref group="xtra">PMID:15840725</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: Amigues, B.]]
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[[Category: Agez M]]
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[[Category: Courbeyrette, R.]]
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[[Category: Amigues B]]
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[[Category: Guerois, R.]]
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[[Category: Courbeyrette R]]
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[[Category: Lautrette, A.]]
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[[Category: Guerois R]]
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[[Category: Mann, C.]]
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[[Category: Lautrette A]]
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[[Category: Mousson, F.]]
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[[Category: Mann C]]
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[[Category: Neumann, J M.]]
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[[Category: Mousson F]]
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[[Category: Ochsenbein, F.]]
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[[Category: Neumann JM]]
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[[Category: Thuret, J Y.]]
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[[Category: Ochsenbein F]]
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[[Category: Beta-sandwich]]
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[[Category: Thuret JY]]
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[[Category: Distorted immunoglobulin-like]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 06:09:10 2009''
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Current revision

NMR structure of human histone chaperone, ASF1A

PDB ID 1tey

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