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5e5a

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Current revision (06:13, 5 July 2023) (edit) (undo)
 
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<StructureSection load='5e5a' size='340' side='right'caption='[[5e5a]], [[Resolution|resolution]] 2.81&Aring;' scene=''>
<StructureSection load='5e5a' size='340' side='right'caption='[[5e5a]], [[Resolution|resolution]] 2.81&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5e5a]] is a 11 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E5A OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5E5A FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5e5a]] is a 11 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens], [https://en.wikipedia.org/wiki/Human_herpesvirus_5_strain_Towne Human herpesvirus 5 strain Towne] 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=5E5A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5E5A FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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]] 2.809&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5e5a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e5a OCA], [http://pdbe.org/5e5a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e5a RCSB], [http://www.ebi.ac.uk/pdbsum/5e5a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5e5a ProSAT]</span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=5e5a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e5a OCA], [https://pdbe.org/5e5a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5e5a RCSB], [https://www.ebi.ac.uk/pdbsum/5e5a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5e5a ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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. [[http://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. [[http://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.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Human herpesvirus 5 strain Towne]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Chen, P]]
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[[Category: Xenopus laevis]]
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[[Category: Fang, J]]
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[[Category: Chen P]]
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[[Category: Fang, Q]]
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[[Category: Fang J]]
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[[Category: Li, G]]
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[[Category: Fang Q]]
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[[Category: Wang, M]]
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[[Category: Li G]]
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[[Category: Xu, R M]]
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[[Category: Wang M]]
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[[Category: Yang, N]]
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[[Category: Xu RM]]
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[[Category: Ctd]]
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[[Category: Yang N]]
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[[Category: Hcmv]]
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[[Category: Ie1]]
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[[Category: Ncp]]
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[[Category: Protein binding-viral protein-dna complex]]
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Current revision

Crystal structure of the chromatin-tethering domain of Human cytomegalovirus IE1 protein bound to the nucleosome core particle

PDB ID 5e5a

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OCA

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