User:Cassandra Marsh/Sandbox 2
From Proteopedia
< User:Cassandra Marsh(Difference between revisions)
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| - | =Histone Deacetylase 8 (HDAC 8), ''H. | + | =Histone Deacetylase 8 (HDAC 8), ''H. sapiens''= |
<StructureSection load='2v5w' size='350' frame='true' side='right' caption='HDAC 8 (PDB:2v5w)' scene=''> | <StructureSection load='2v5w' size='350' frame='true' side='right' caption='HDAC 8 (PDB:2v5w)' scene=''> | ||
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==Introduction== | ==Introduction== | ||
===Histones=== | ===Histones=== | ||
| - | [https://en.wikipedia.org/wiki/Histone Histones] are a family of basic, positively charged proteins that associate with DNA inside the nucleus to help condense the DNA into [https://en.wikipedia.org/wiki/Chromatin chromatin] <ref name="Histones"> Histones | Learn Science at Scitable https://www.nature.com/scitable/definition/histone-histones-57</ref>. The nuclear DNA is wrapped around the histone in order to fit in the nucleus. [https://en.wikipedia.org/wiki/Nucleosome Nucleosomes] are chromatin beads made up of DNA wrapped around eight histone proteins, or a [https://en.wikipedia.org/wiki/Histone_octamer histone octamer] <ref name="Histones" />. The modification of histones are a type of [https://en.wikipedia.org/wiki/Epigenetics | + | [https://en.wikipedia.org/wiki/Histone Histones] are a family of basic, positively charged proteins that associate with DNA inside the nucleus to help condense the DNA into [https://en.wikipedia.org/wiki/Chromatin chromatin] <ref name="Histones"> Histones | Learn Science at Scitable https://www.nature.com/scitable/definition/histone-histones-57</ref>. The nuclear DNA is wrapped around the histone in order to fit in the nucleus. [https://en.wikipedia.org/wiki/Nucleosome Nucleosomes] are chromatin beads made up of DNA wrapped around eight histone proteins, or a [https://en.wikipedia.org/wiki/Histone_octamer histone octamer] <ref name="Histones" />. The modification of histones are a type of [https://en.wikipedia.org/wiki/Epigenetics epigenetics], where changes are made in gene expression without altering the DNA sequence. Four different examples of modifying histones including [https://en.wikipedia.org/wiki/Histone_acetylation_and_deacetylation Histone acetylation, Histone deacetylation], [https://en.wikipedia.org/wiki/Histone_methylation Histone methylation] and [https://en.wikipedia.org/wiki/Demethylase Histone demethylation] <ref name="Histones" />. |
===Histone Deacetylases (HDACs)=== | ===Histone Deacetylases (HDACs)=== | ||
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====HDAC8==== | ====HDAC8==== | ||
| - | [https://en.wikipedia.org/wiki/HDAC8 Histone Deacetylase 8] is | + | [https://en.wikipedia.org/wiki/HDAC8 Histone Deacetylase 8] is an enzyme found in ''[https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]''. HDAC8 is 388 residues long and consists of eight-stranded parallel β-sheets surrounded by 11 α-helices <ref name="Vanninni" />. HDAC8 is the only functional HDAC that is found to be a single polypeptide instead of being high-molecular-weight multi-protein complexes <ref name="Vanninni" />. The substrate bound to the HDAC8 includes an acetyl group, one arginine, one histidine, two lysines and MCM, a Coumarin fluorescence tag. |
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===Potassium Binding Site=== | ===Potassium Binding Site=== | ||
| + | There are two potassium ions in HDAC8. While their exact function is unknown, these ions do increase the catalytic activity and stability of the enzyme overall. The potassium ion closest to the active site becomes a <scene name='81/812841/Potassium_binding_site/5'>Potassium Binding Site</scene>. The potassium ion octahedrally coordinates with the side chain oxygen of S199 and D176 and the backbone oxygen of D176, D178, H180 and L200 <ref name="Chen">PMID:25060069</ref>. Because the second potassium ion is about 20 Å from the catalytic center, this only regulates the enzymatic activity by an allosteric effect <ref name="Chen" />. | ||
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==Deacetylation== | ==Deacetylation== | ||
Current revision
Histone Deacetylase 8 (HDAC 8), H. sapiens
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References
- ↑ 1.0 1.1 1.2 Histones | Learn Science at Scitable https://www.nature.com/scitable/definition/histone-histones-57
- ↑ 2.0 2.1 2.2 2.3 2.4 Vannini A, Volpari C, Gallinari P, Jones P, Mattu M, Carfi A, De Francesco R, Steinkuhler C, Di Marco S. Substrate binding to histone deacetylases as shown by the crystal structure of the HDAC8-substrate complex. EMBO Rep. 2007 Sep;8(9):879-84. Epub 2007 Aug 10. PMID:17721440
- ↑ 3.0 3.1 Chen K, Zhang X, Wu YD, Wiest O. Inhibition and mechanism of HDAC8 revisited. J Am Chem Soc. 2014 Aug 20;136(33):11636-43. doi: 10.1021/ja501548p. Epub 2014, Aug 7. PMID:25060069 doi:http://dx.doi.org/10.1021/ja501548p
Student Contributors
- Cassandra Marsh
- Courtney Brown
- Carolyn Hurdle
