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1p3m

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Current revision (09:36, 16 August 2023) (edit) (undo)
 
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<StructureSection load='1p3m' size='340' side='right'caption='[[1p3m]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
<StructureSection load='1p3m' size='340' side='right'caption='[[1p3m]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1p3m]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/ ] and [https://en.wikipedia.org/wiki/African_clawed_frog African clawed frog]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P3M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P3M FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1p3m]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P3M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P3M FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1aoi|1aoi]], [[1f66|1f66]], [[1id3|1id3]], [[1kx3|1kx3]], [[1kx4|1kx4]], [[1kx5|1kx5]], [[1p34|1p34]], [[1p3a|1p3a]], [[1p3b|1p3b]], [[1p3f|1p3f]], [[1p3g|1p3g]], [[1p3i|1p3i]], [[1p3k|1p3k]], [[1p3l|1p3l]], [[1p3o|1p3o]], [[1p3p|1p3p]]</div></td></tr>
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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]] 2.9&#8491;</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=1p3m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p3m OCA], [https://pdbe.org/1p3m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p3m RCSB], [https://www.ebi.ac.uk/pdbsum/1p3m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p3m 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=1p3m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p3m OCA], [https://pdbe.org/1p3m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p3m RCSB], [https://www.ebi.ac.uk/pdbsum/1p3m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p3m ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://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. [[https://www.uniprot.org/uniprot/H2B11_XENLA H2B11_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.
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[https://www.uniprot.org/uniprot/H32_XENLA H32_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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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: African clawed frog]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Bao, Y]]
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[[Category: Xenopus laevis]]
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[[Category: Dyer, P N]]
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[[Category: Bao Y]]
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[[Category: Edayathumangalam, R S]]
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[[Category: Dyer PN]]
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[[Category: Forsberg, L J]]
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[[Category: Edayathumangalam RS]]
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[[Category: Luger, K]]
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[[Category: Forsberg LJ]]
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[[Category: Muthurajan, U M]]
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[[Category: Luger K]]
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[[Category: White, C L]]
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[[Category: Muthurajan UM]]
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[[Category: Chromatin]]
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[[Category: White CL]]
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[[Category: Nucleosome core particle]]
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[[Category: Protein/dna interaction]]
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[[Category: Sin mutant]]
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[[Category: Structural protein-dna complex]]
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Current revision

Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants

PDB ID 1p3m

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OCA

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