Sandbox GGC1

From Proteopedia

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'''Histone H3.3'''
'''Histone H3.3'''
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<StructureSection load='ASF1A' size='340' side='right' caption='Caption for this structure' scene=''>
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<StructureSection load='H3-3A' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page '''Sandbox GGC1'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
This is a default text for your page '''Sandbox GGC1'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
== Function ==
== Function ==
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[https://www.uniprot.org/uniprot/P84243]. The Variant [https://www.uniprot.org/uniprot/P84243 histone H3] replaces H3 in a range of nucleosomes in active genes. Deposited at sites of nucleosomal displacement throughout transcribed genes, suggesting that it represents an epigenetic imprint of transcriptionally active chromatin. 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
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The Variant [https://www.uniprot.org/uniprot/P84243 histone H3] replaces H3 in a range of nucleosomes in active genes. Deposited at sites of nucleosomal displacement throughout transcribed genes which represents an epigenetic imprint of active chromatin. Nucleosomes wrap and compact DNA into chromatin. Also Histones 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
== Disease ==
== Disease ==
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== Structural highlights ==
== Structural highlights ==
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in a PubMed abstract,[https://www.nature.com/articles/srep07115 CENP-A]which is a centromere-specific histone H3 variant is over expressed in cancer cells and it can be mislocalized ectopically in the form of heterotypic nucleosomes containing H3.3.
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This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
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</StructureSection>
</StructureSection>

Revision as of 14:09, 16 September 2020

Histone H3.3

Caption for this structure

Drag the structure with the mouse to rotate

References

1. H3C15 - Histone H3.2 - Homo sapiens (Human) - H3C15 gene & protein https://www.uniprot.org/uniprot/Q71DI3 (accessed Sep 15, 2020)

  1. ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
  2. ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
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