5ay8: Difference between revisions

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 <StructureSection load='5ay8' size='340' side='right'caption='[[5ay8]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5ay8]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AY8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AY8 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5ay8]] is a 10 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=5AY8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AY8 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HIST1H4A, H4/A, H4FA, HIST1H4B, H4/I, H4FI, HIST1H4C, H4/G, H4FG, HIST1H4D, H4/B, H4FB, HIST1H4E, H4/J, H4FJ, HIST1H4F, H4/C, H4FC, HIST1H4H, H4/H, H4FH, HIST1H4I, H4/M, H4FM, HIST1H4J, H4/E, H4FE, HIST1H4K, H4/D, H4FD, HIST1H4L, H4/K, H4FK, HIST2H4A, H4/N, H4F2, H4FN, HIST2H4, HIST2H4B, H4/O, H4FO, HIST4H4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), HIST1H2AB, H2AFM, HIST1H2AE, H2AFA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), HIST1H2BJ, H2BFR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ay8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ay8 OCA], [http://pdbe.org/5ay8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ay8 RCSB], [http://www.ebi.ac.uk/pdbsum/5ay8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ay8 ProSAT]</span></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=5ay8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ay8 OCA], [https://pdbe.org/5ay8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ay8 RCSB], [https://www.ebi.ac.uk/pdbsum/5ay8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ay8 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/H2B1J_HUMAN H2B1J_HUMAN]] Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.<ref>PMID:11859126</ref> <ref>PMID:12860195</ref> <ref>PMID:15019208</ref>   Has broad antibacterial activity. May contribute to the formation of the functional antimicrobial barrier of the colonic epithelium, and to the bactericidal activity of amniotic fluid.<ref>PMID:11859126</ref> <ref>PMID:12860195</ref> <ref>PMID:15019208</ref>
+[https://www.uniprot.org/uniprot/H3Y1_HUMAN H3Y1_HUMAN] Primate-specific variant histone H3, which constitutes a core component of nucleosomes (PubMed:20819935, PubMed:27016736). Histone H3.Y-containing nucleosomes accumulate around transcription start sites and have flexible DNA ends, suggesting that they form relaxed chromatin that allows transcription factor access (PubMed:27016736). Histone H1 binds less efficiently to histone H3.Y-containing nucleosomes (PubMed:27016736). Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling (Probable).<ref>PMID:20819935</ref> <ref>PMID:27016736</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
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 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Horikoshi, N]]
+[[Category: Horikoshi N]]
-[[Category: Kimura, H]]
+[[Category: Kimura H]]
-[[Category: Kujirai, T]]
+[[Category: Kujirai T]]
-[[Category: Kurumizaka, H]]
+[[Category: Kurumizaka H]]
-[[Category: Machida, S]]
+[[Category: Machida S]]
-[[Category: Maehara, K]]
+[[Category: Maehara K]]
-[[Category: Ohkawa, Y]]
+[[Category: Ohkawa Y]]
-[[Category: Osakabe, A]]
+[[Category: Osakabe A]]
-[[Category: Sato, K]]
+[[Category: Sato K]]
-[[Category: Dna binding protein-dna complex]]
-[[Category: Histone fold dna binding nucleus]]