5b33: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
 
(One intermediate revision by the same user not shown)
Line 3: Line 3:
<StructureSection load='5b33' size='340' side='right'caption='[[5b33]], [[Resolution|resolution]] 2.92&Aring;' scene=''>
<StructureSection load='5b33' size='340' side='right'caption='[[5b33]], [[Resolution|resolution]] 2.92&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5b33]] is a 10 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B33 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5B33 FirstGlance]. <br>
<table><tr><td colspan='2'>[[5b33]] is a 10 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=5B33 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5B33 FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5b32|5b32]], [[5b31|5b31]]</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]] 2.925&#8491;</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=5b33 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b33 OCA], [http://pdbe.org/5b33 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5b33 RCSB], [http://www.ebi.ac.uk/pdbsum/5b33 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5b33 ProSAT]</span></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=5b33 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b33 OCA], [https://pdbe.org/5b33 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5b33 RCSB], [https://www.ebi.ac.uk/pdbsum/5b33 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5b33 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[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>  [[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> 
[https://www.uniprot.org/uniprot/H33_HUMAN H33_HUMAN]  
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 25: Line 25:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Arimura, Y]]
[[Category: Arimura Y]]
[[Category: Horikoshi, N]]
[[Category: Horikoshi N]]
[[Category: Kurumizaka, H]]
[[Category: Kurumizaka H]]
[[Category: Taguchi, H]]
[[Category: Taguchi H]]
[[Category: Dna binding protein]]
[[Category: Histone variant]]
[[Category: Nucleosome]]
[[Category: Protein-dna complex]]

Latest revision as of 15:58, 8 November 2023

The crystal structure of the H2AZ nucleosome with H3.3.

5b33, resolution 2.92Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA