2xd7: Difference between revisions

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<StructureSection load='2xd7' size='340' side='right'caption='[[2xd7]], [[Resolution|resolution]] 2.09&Aring;' scene=''>
<StructureSection load='2xd7' size='340' side='right'caption='[[2xd7]], [[Resolution|resolution]] 2.09&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2xd7]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XD7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XD7 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2xd7]] is a 4 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=2XD7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XD7 FirstGlance]. <br>
</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=2xd7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xd7 OCA], [https://pdbe.org/2xd7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xd7 RCSB], [https://www.ebi.ac.uk/pdbsum/2xd7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xd7 ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.09&#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=2xd7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xd7 OCA], [https://pdbe.org/2xd7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xd7 RCSB], [https://www.ebi.ac.uk/pdbsum/2xd7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xd7 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/H2AW_HUMAN H2AW_HUMAN]] Variant histone H2A which replaces conventional H2A in a subset of nucleosomes where it represses transcription. 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 stable X chromosome inactivation.<ref>PMID:15621527</ref>
[https://www.uniprot.org/uniprot/H2AW_HUMAN H2AW_HUMAN] Variant histone H2A which replaces conventional H2A in a subset of nucleosomes where it represses transcription. 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 stable X chromosome inactivation.<ref>PMID:15621527</ref>  
== 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>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Arrowsmith, C H]]
[[Category: Arrowsmith CH]]
[[Category: Bountra, C]]
[[Category: Bountra C]]
[[Category: Carpenter, E P]]
[[Category: Carpenter EP]]
[[Category: Delft, F von]]
[[Category: Edwards A]]
[[Category: Edwards, A]]
[[Category: Gileadi O]]
[[Category: Gileadi, O]]
[[Category: Krojer T]]
[[Category: Krojer, T]]
[[Category: Muniz JRC]]
[[Category: Muniz, J R.C]]
[[Category: Phillips C]]
[[Category: Phillips, C]]
[[Category: Ugochukwu E]]
[[Category: Ugochukwu, E]]
[[Category: Vollmar M]]
[[Category: Vollmar, M]]
[[Category: Weigelt J]]
[[Category: Weigelt, J]]
[[Category: Von Delft F]]
[[Category: Chromatin regulator]]
[[Category: Chromosomal protein]]
[[Category: Dna binding protein]]
[[Category: Dna-binding protein]]
[[Category: Nucleosome core]]
[[Category: Nucleus]]
[[Category: Phosphoprotein]]

Latest revision as of 13:29, 20 December 2023

Crystal structure of the macro domain of human core histone H2ACrystal structure of the macro domain of human core histone H2A

Structural highlights

2xd7 is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.09Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

H2AW_HUMAN Variant histone H2A which replaces conventional H2A in a subset of nucleosomes where it represses transcription. 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 stable X chromosome inactivation.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Zhang R, Poustovoitov MV, Ye X, Santos HA, Chen W, Daganzo SM, Erzberger JP, Serebriiskii IG, Canutescu AA, Dunbrack RL, Pehrson JR, Berger JM, Kaufman PD, Adams PD. Formation of MacroH2A-containing senescence-associated heterochromatin foci and senescence driven by ASF1a and HIRA. Dev Cell. 2005 Jan;8(1):19-30. PMID:15621527 doi:S1534580704004083

2xd7, resolution 2.09Å

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