3c1c
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3c1c]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Eukaryota Eukaryota] and [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C1C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3C1C FirstGlance]. <br> | <table><tr><td colspan='2'>[[3c1c]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Eukaryota Eukaryota] and [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C1C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3C1C FirstGlance]. <br> | ||
- | </td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=M2L:(2R)-2-AMINO-3-(2-DIMETHYLAMINOETHYLSULFANYL)PROPANOIC+ACID'>M2L</scene></td></tr> | + | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=M2L:(2R)-2-AMINO-3-(2-DIMETHYLAMINOETHYLSULFANYL)PROPANOIC+ACID'>M2L</scene></td></tr> |
- | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1kx5|1kx5]], [[1aoi|1aoi]], [[1zla|1zla]], [[1kx3|1kx3]], [[1f66|1f66]], [[1kx4|1kx4]], [[3c1b|3c1b]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1kx5|1kx5]], [[1aoi|1aoi]], [[1zla|1zla]], [[1kx3|1kx3]], [[1f66|1f66]], [[1kx4|1kx4]], [[3c1b|3c1b]]</td></tr> |
- | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Histone H3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8355 Xenopus laevis]), Histone H4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8355 Xenopus laevis]), Histone H2A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8355 Xenopus laevis]), hist2h2bf, TGas058p09.1-001 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2759 Eukaryota])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Histone H3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8355 Xenopus laevis]), Histone H4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8355 Xenopus laevis]), Histone H2A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8355 Xenopus laevis]), hist2h2bf, TGas058p09.1-001 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2759 Eukaryota])</td></tr> |
- | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3c1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c1c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3c1c RCSB], [http://www.ebi.ac.uk/pdbsum/3c1c PDBsum]</span></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=3c1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c1c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3c1c RCSB], [http://www.ebi.ac.uk/pdbsum/3c1c PDBsum]</span></td></tr> |
- | <table> | + | </table> |
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/H3L_XENLA H3L_XENLA]] 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. [[http://www.uniprot.org/uniprot/H2A1_XENLA H2A1_XENLA]] 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. [[http://www.uniprot.org/uniprot/H4_XENLA H4_XENLA]] 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. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Eukaryota]] | [[Category: Eukaryota]] | ||
[[Category: Xenopus laevis]] | [[Category: Xenopus laevis]] | ||
- | [[Category: Chodaparambil, J | + | [[Category: Chodaparambil, J]] |
- | [[Category: Hansen, J | + | [[Category: Hansen, J]] |
- | [[Category: Lu, X | + | [[Category: Lu, X]] |
- | [[Category: Luger, K | + | [[Category: Luger, K]] |
- | [[Category: Shokat, K | + | [[Category: Shokat, K]] |
- | [[Category: Simon, M | + | [[Category: Simon, M]] |
[[Category: Chromatin]] | [[Category: Chromatin]] | ||
[[Category: Chromosomal protein]] | [[Category: Chromosomal protein]] |
Revision as of 18:09, 24 December 2014
The effect of H3 K79 dimethylation and H4 K20 trimethylation on nucleosome and chromatin structure
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Categories: Eukaryota | Xenopus laevis | Chodaparambil, J | Hansen, J | Lu, X | Luger, K | Shokat, K | Simon, M | Chromatin | Chromosomal protein | Dna-binding | Histone h3 | Histone modification | Methylation | Nucleosomal array | Nucleosomal surface | Nucleosome | Nucleosome core | Nucleus | Phosphoprotein | Structural protein-dna complex | Trimethylation