5e5a: Difference between revisions

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'''Unreleased structure'''


The entry 5e5a is ON HOLD
==Crystal structure of the chromatin-tethering domain of Human cytomegalovirus IE1 protein bound to the nucleosome core particle==
<StructureSection load='5e5a' size='340' side='right'caption='[[5e5a]], [[Resolution|resolution]] 2.81&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
<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>
== Function ==
[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;">
== Publication Abstract from PubMed ==
Human cytomegalovirus (hCMV) immediate early 1 (IE1) protein associates with condensed chromatin of the host cell during mitosis. We have determined the structure of the chromatin-tethering domain (CTD) of IE1 bound to the nucleosome core particle, and discovered that IE1-CTD specifically interacts with the H2A-H2B acidic patch and impairs the compaction of higher-order chromatin structure. Our results suggest that IE1 loosens up the folding of host chromatin during hCMV infections.


Authors: Fang, Q., Chen, P., Wang, M., Fang, J., Yang, N., Li, G., Xu, R.M.
Human cytomegalovirus IE1 protein alters the higher-order chromatin structure by targeting the acidic patch of the nucleosome.,Fang Q, Chen P, Wang M, Fang J, Yang N, Li G, Xu RM Elife. 2016 Jan 26;5. pii: e11911. doi: 10.7554/eLife.11911. PMID:26812545<ref>PMID:26812545</ref>


Description: Crystal structure of NCP-protein complex
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Wang, M]]
<div class="pdbe-citations 5e5a" style="background-color:#fffaf0;"></div>
[[Category: Chen, P]]
 
[[Category: Fang, Q]]
==See Also==
[[Category: Li, G]]
*[[Histone 3D structures|Histone 3D structures]]
[[Category: Xu, R.M]]
== References ==
[[Category: Yang, N]]
<references/>
[[Category: Fang, J]]
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Human herpesvirus 5 strain Towne]]
[[Category: Large Structures]]
[[Category: Xenopus laevis]]
[[Category: Chen P]]
[[Category: Fang J]]
[[Category: Fang Q]]
[[Category: Li G]]
[[Category: Wang M]]
[[Category: Xu RM]]
[[Category: Yang N]]