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4cay

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Revision as of 17:35, 7 September 2022

Crystal structure of a human Anp32e-H2A.Z-H2B complex

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OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4cay"

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 <StructureSection load='4cay' size='340' side='right'caption='[[4cay]], [[Resolution|resolution]] 1.48&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4cay]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CAY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CAY FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4cay]] is a 3 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=4CAY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CAY FirstGlance]. <br>
-</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=4cay FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cay OCA], [http://pdbe.org/4cay PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cay RCSB], [http://www.ebi.ac.uk/pdbsum/4cay PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cay ProSAT]</span></td></tr>
+</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=4cay FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cay OCA], [https://pdbe.org/4cay PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cay RCSB], [https://www.ebi.ac.uk/pdbsum/4cay PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cay ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/H2AZ_HUMAN H2AZ_HUMAN]] Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. 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. May be involved in the formation of constitutive heterochromatin. May be required for chromosome segregation during cell division.<ref>PMID:15878876</ref>  [[http://www.uniprot.org/uniprot/AN32E_HUMAN AN32E_HUMAN]] Inhibits activity of protein phosphatase 2A (PP2A). Does not inhibit protein phosphatase 1. May play a role in cerebellar development and synaptogenesis process by modulating PP2A activity (By similarity). [[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/H2AZ_HUMAN H2AZ_HUMAN]] Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. 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. May be involved in the formation of constitutive heterochromatin. May be required for chromosome segregation during cell division.<ref>PMID:15878876</ref>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-H2A.Z is an essential histone variant implicated in the regulation of key nuclear events. However, the metazoan chaperones responsible for H2A.Z deposition and its removal from chromatin remain unknown. Here we report the identification and characterization of the human protein ANP32E as a specific H2A.Z chaperone. We show that ANP32E is a member of the presumed H2A.Z histone-exchange complex p400/TIP60. ANP32E interacts with a short region of the docking domain of H2A.Z through a new motif termed H2A.Z interacting domain (ZID). The 1.48 A resolution crystal structure of the complex formed between the ANP32E-ZID and the H2A.Z/H2B dimer and biochemical data support an underlying molecular mechanism for H2A.Z/H2B eviction from the nucleosome and its stabilization by ANP32E through a specific extension of the H2A.Z carboxy-terminal alpha-helix. Finally, analysis of H2A.Z localization in ANP32E(-/-) cells by chromatin immunoprecipitation followed by sequencing shows genome-wide enrichment, redistribution and accumulation of H2A.Z at specific chromatin control regions, in particular at enhancers and insulators.
-ANP32E is a histone chaperone that removes H2A.Z from chromatin.,Obri A, Ouararhni K, Papin C, Diebold ML, Padmanabhan K, Marek M, Stoll I, Roy L, Reilly PT, Mak TW, Dimitrov S, Romier C, Hamiche A Nature. 2014 Jan 30;505(7485):648-53. doi: 10.1038/nature12922. Epub 2014 Jan 22. PMID:24463511<ref>PMID:24463511</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 4cay" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Histone|Histone]]
+*[[Histone 3D structures|Histone 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Diebold, M L]]
+[[Category: Diebold M-L]]
-[[Category: Dimitrov, S]]
+[[Category: Dimitrov S]]
-[[Category: Hamiche, A]]
+[[Category: Hamiche A]]
-[[Category: Mak, T W]]
+[[Category: Mak TW]]
-[[Category: Marek, M]]
+[[Category: Marek M]]
-[[Category: Obri, A]]
+[[Category: Obri A]]
-[[Category: Ouararhni, K]]
+[[Category: Ouararhni K]]
-[[Category: Padmanabhan, K]]
+[[Category: Padmanabhan K]]
-[[Category: Papin, C]]
+[[Category: Papin C]]
-[[Category: Reilly, P T]]
+[[Category: Reilly PT]]
-[[Category: Romier, C]]
+[[Category: Romier C]]
-[[Category: Roy, L]]
+[[Category: Roy L]]
-[[Category: Stoll, I]]
+[[Category: Stoll I]]
-[[Category: Epigenetic]]
-[[Category: Histone chaperone]]
-[[Category: Histone variant]]
-[[Category: Nucleosome]]
-[[Category: Transcription]]

4cay

From Proteopedia

Revision as of 17:35, 7 September 2022

Crystal structure of a human Anp32e-H2A.Z-H2B complex

Structural highlights

Function

See Also

References

Contents

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