6fy5: Difference between revisions

Line 1:

~~'''Unreleased structure'''~~

~~The entry~~ 6fy5 is ~~ON HOLD~~

==Crystal structure of the macro domain of human macroh2a2==

~~Authors~~: ~~Hothorn~~, M.

== Structural highlights ==

<table><tr><td colspan='2'>[[6fy5]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FY5 OCA]. For a guided tour on the structure components use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FY5 FirstGlance].

~~Description: Crystal structure of the macro domain of human macroh2a2~~

</td></tr><tr id='ligand'><td class="sblockLbl">[[Ligand|Ligands:]]</td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>

[[~~Category~~: ~~Unreleased Structures~~]]

<tr id='related'><td class="sblockLbl">[[Related_structure|Related:]]</td><td class="sblockDat">[[1zr3|1zr3]]</td></tr>

<tr id='resources'><td class="sblockLbl">Resources:</td><td class="sblockDat">[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6fy5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fy5 OCA], [http://pdbe.org/6fy5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fy5 RCSB], [http://www.ebi.ac.uk/pdbsum/6fy5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fy5 ProSAT]</td></tr>

</table>

== Function ==

[[http://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>

== References ==

__TOC__

</StructureSection>

[[Category: Hothorn, M]]

[[Category: Dna binding protein]]

[[Category: Histone variant]]

[[Category: Macro domain]]

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-'''Unreleased structure'''
-The entry 6fy5 is ON HOLD
+==Crystal structure of the macro domain of human macroh2a2==
+<StructureSection load='6fy5' size='340' side='right' caption='[[6fy5]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
-Authors: Hothorn, M.
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6fy5]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FY5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FY5 FirstGlance]. <br>
-Description: Crystal structure of the macro domain of human macroh2a2
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
-[[Category: Unreleased Structures]]
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1zr3|1zr3]]</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=6fy5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fy5 OCA], [http://pdbe.org/6fy5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fy5 RCSB], [http://www.ebi.ac.uk/pdbsum/6fy5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fy5 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://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>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Hothorn, M]]
+[[Category: Dna binding protein]]
+[[Category: Histone variant]]
+[[Category: Macro domain]]