https://proteopedia.org/api.php?action=feedcontributions&feedformat=atom&user=Cassandra+MarshProteopedia - User contributions [en]2026-09-24T12:11:01ZUser contributionsMediaWiki 1.43.8https://proteopedia.org/index.php?title=File:Hdac8finalmechanism.PNG&diff=3029881File:Hdac8finalmechanism.PNG2019-04-19T17:28:15Z<p>Cassandra Marsh: </p>
<hr />
<div></div>Cassandra Marshhttps://proteopedia.org/index.php?title=User:Cassandra_Marsh/Sandbox_2&diff=3022762User:Cassandra Marsh/Sandbox 22019-04-07T01:49:26Z<p>Cassandra Marsh: </p>
<hr />
<div>=Histone Deacetylase 8 (HDAC 8), ''H. sapiens''=<br />
<StructureSection load='2v5w' size='350' frame='true' side='right' caption='HDAC 8 (PDB:2v5w)' scene=''><br />
<br />
<br />
==Introduction==<br />
===Histones===<br />
[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" />. <br />
<br />
===Histone Deacetylases (HDACs)===<br />
ε-Amino-lysine acetylation is a type of histone modification that controls the stability of proteins and biological function in eukaryotic cells <ref name="Vanninni">PMID:17721440</ref>. Histone Deacetylation is the reversal process for this acetylation modification. There are different classes of HDACs based on phylogenetic analysis:<br />
<br />
•Class I - HDACs 1-3 and 8, which are homologous to yeast Rpd3<br />
<br />
•Class II - HDACs 4-7, 9 and 10, which are homologous to yeast Hda1<br />
<br />
•Class III - Sirtuin deacetylases <br />
<br />
•Class IV - HDAC 11 <ref name="Vanninni" />.<br />
<br />
HDACs 1-11 are metalloenzymes and require a zinc ion for deacetylation <ref name="Vanninni" />. <br />
<br />
====HDAC8====<br />
[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.<br />
<br />
<br />
<br />
<br />
==Structure==<br />
<br />
===General Structure Information===<br />
<br />
===Inhibitor===<br />
<br />
===Potassium Binding Site===<br />
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" />.<br />
<br />
<br />
==Deacetylation==<br />
<br />
===Zn<sup>2+</sup> Metal Ion Mechanism===<br />
[[Image:Hdac mech.PNG|400 px|left|thumb|Figure 1. Mechanism of HDAC8]]<br />
<br />
===Active Site===<br />
<br />
==Disease==<br />
[https://friedreichsataxianews.com/friedreichs-ataxia-experimental-treatments/histone-deacetylase-inhibitors/ HDACis]<br />
<br />
<br />
</StructureSection><br />
== References ==<br />
<references/><br />
==Student Contributors==<br />
*Cassandra Marsh<br />
*Courtney Brown<br />
*Carolyn Hurdle</div>Cassandra Marshhttps://proteopedia.org/index.php?title=User:Cassandra_Marsh/Sandbox_2&diff=3022761User:Cassandra Marsh/Sandbox 22019-04-07T01:26:39Z<p>Cassandra Marsh: </p>
<hr />
<div>=Histone Deacetylase 8 (HDAC 8), ''H. sapiens''=<br />
<StructureSection load='2v5w' size='350' frame='true' side='right' caption='HDAC 8 (PDB:2v5w)' scene=''><br />
<br />
<br />
==Introduction==<br />
===Histones===<br />
[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" />. <br />
<br />
===Histone Deacetylases (HDACs)===<br />
ε-Amino-lysine acetylation is a type of histone modification that controls the stability of proteins and biological function in eukaryotic cells <ref name="Vanninni">PMID:17721440</ref>. Histone Deacetylation is the reversal process for this acetylation modification. There are different classes of HDACs based on phylogenetic analysis:<br />
<br />
•Class I - HDACs 1-3 and 8, which are homologous to yeast Rpd3<br />
<br />
•Class II - HDACs 4-7, 9 and 10, which are homologous to yeast Hda1<br />
<br />
•Class III - Sirtuin deacetylases <br />
<br />
•Class IV - HDAC 11 <ref name="Vanninni" />.<br />
<br />
HDACs 1-11 are metalloenzymes and require a zinc ion for deacetylation <ref name="Vanninni" />. <br />
<br />
====HDAC8====<br />
[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.<br />
<br />
<br />
<br />
<br />
==Structure==<br />
<br />
===General Structure Information===<br />
<br />
===Inhibitor===<br />
<br />
===Potassium Binding Site===<br />
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/4'>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" />.<br />
<br />
<br />
==Deacetylation==<br />
<br />
===Zn<sup>2+</sup> Metal Ion Mechanism===<br />
[[Image:Hdac mech.PNG|400 px|left|thumb|Figure 1. Mechanism of HDAC8]]<br />
<br />
===Active Site===<br />
<br />
==Disease==<br />
[https://friedreichsataxianews.com/friedreichs-ataxia-experimental-treatments/histone-deacetylase-inhibitors/ HDACis]<br />
<br />
<br />
</StructureSection><br />
== References ==<br />
<references/><br />
==Student Contributors==<br />
*Cassandra Marsh<br />
*Courtney Brown<br />
*Carolyn Hurdle</div>Cassandra Marshhttps://proteopedia.org/index.php?title=User:Cassandra_Marsh/Sandbox_2&diff=3022742User:Cassandra Marsh/Sandbox 22019-04-06T22:49:13Z<p>Cassandra Marsh: </p>
<hr />
<div>=Histone Deacetylase 8 (HDAC 8), ''H. sapiens''=<br />
<StructureSection load='2v5w' size='350' frame='true' side='right' caption='HDAC 8 (PDB:2v5w)' scene=''><br />
<br />
<br />
==Introduction==<br />
===Histones===<br />
[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" />. <br />
<br />
===Histone Deacetylases (HDACs)===<br />
ε-Amino-lysine acetylation is a type of histone modification that controls the stability of proteins and biological function in eukaryotic cells <ref name="Vanninni">PMID:17721440</ref>. Histone Deacetylation is the reversal process for this acetylation modification. There are different classes of HDACs based on phylogenetic analysis:<br />
<br />
•Class I - HDACs 1-3 and 8, which are homologous to yeast Rpd3<br />
<br />
•Class II - HDACs 4-7, 9 and 10, which are homologous to yeast Hda1<br />
<br />
•Class III - Sirtuin deacetylases <br />
<br />
•Class IV - HDAC 11 <ref name="Vanninni" />.<br />
<br />
HDACs 1-11 are metalloenzymes and require a zinc ion for deacetylation <ref name="Vanninni" />. <br />
<br />
====HDAC8====<br />
[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.<br />
<br />
<br />
<br />
<br />
==Structure==<br />
<br />
===General Structure Information===<br />
<br />
===Inhibitor===<br />
<br />
===Potassium Binding Site===<br />
There are two potassium ions in HDAC8. While their exact function is unknown, these ions do increase the catalytic activity of the enzyme overall. The potassium ion closest to the active site becomes a <scene name='81/812841/Potassium_binding_site/4'>Potassium Binding Site</scene><br />
==Deacetylation==<br />
<br />
===Zn<sup>2+</sup> Metal Ion Mechanism===<br />
[[Image:Hdac mech.PNG|400 px|left|thumb|Figure 1. Mechanism of HDAC8]]<br />
<br />
===Active Site===<br />
<br />
==Disease==<br />
[https://friedreichsataxianews.com/friedreichs-ataxia-experimental-treatments/histone-deacetylase-inhibitors/ HDACis]<br />
<br />
<br />
</StructureSection><br />
== References ==<br />
<references/><br />
==Student Contributors==<br />
*Cassandra Marsh<br />
*Courtney Brown<br />
*Carolyn Hurdle</div>Cassandra Marshhttps://proteopedia.org/index.php?title=User:Cassandra_Marsh/Sandbox_2&diff=3022741User:Cassandra Marsh/Sandbox 22019-04-06T22:29:21Z<p>Cassandra Marsh: </p>
<hr />
<div>=Histone Deacetylase 8 (HDAC 8), ''H. sapiens''=<br />
<StructureSection load='2v5w' size='350' frame='true' side='right' caption='HDAC 8 (PDB:2v5w)' scene=''><br />
<br />
<br />
==Introduction==<br />
===Histones===<br />
[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" />. <br />
<br />
===Histone Deacetylases (HDACs)===<br />
ε-Amino-lysine acetylation is a type of histone modification that controls the stability of proteins and biological function in eukaryotic cells <ref name="Vanninni">PMID:17721440</ref>. Histone Deacetylation is the reversal process for this acetylation modification. There are different classes of HDACs based on phylogenetic analysis:<br />
<br />
•Class I - HDACs 1-3 and 8, which are homologous to yeast Rpd3<br />
<br />
•Class II - HDACs 4-7, 9 and 10, which are homologous to yeast Hda1<br />
<br />
•Class III - Sirtuin deacetylases <br />
<br />
•Class IV - HDAC 11 <ref name="Vanninni" />.<br />
<br />
HDACs 1-11 are metalloenzymes and require a zinc ion for deacetylation <ref name="Vanninni" />. <br />
<br />
====HDAC8====<br />
[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.<br />
<br />
<br />
<br />
<br />
==Structure==<br />
<br />
===General Structure Information===<br />
<br />
===Inhibitor===<br />
<br />
===Potassium Binding Site===<br />
<scene name='81/812841/Potassium_binding_site/4'>Potassium Binding Site</scene><br />
==Deacetylation==<br />
<br />
===Zn<sup>2+</sup> Metal Ion Mechanism===<br />
[[Image:Hdac mech.PNG|400 px|left|thumb|Figure 1. Mechanism of HDAC8]]<br />
<br />
===Active Site===<br />
<br />
==Disease==<br />
[https://friedreichsataxianews.com/friedreichs-ataxia-experimental-treatments/histone-deacetylase-inhibitors/ HDACis]<br />
<br />
<br />
</StructureSection><br />
== References ==<br />
<references/><br />
==Student Contributors==<br />
*Cassandra Marsh<br />
*Courtney Brown<br />
*Carolyn Hurdle</div>Cassandra Marshhttps://proteopedia.org/index.php?title=User:Cassandra_Marsh/Sandbox_2&diff=3022739User:Cassandra Marsh/Sandbox 22019-04-06T22:09:14Z<p>Cassandra Marsh: </p>
<hr />
<div>=Histone Deacetylase 8 (HDAC 8), ''H. sapiens''=<br />
<StructureSection load='2v5w' size='350' frame='true' side='right' caption='HDAC 8 (PDB:2v5w)' scene=''><br />
<br />
<br />
==Introduction==<br />
===Histones===<br />
[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" />. <br />
<br />
===Histone Deacetylases (HDACs)===<br />
ε-Amino-lysine acetylation is a type of histone modification that controls the stability of proteins and biological function in eukaryotic cells <ref name="Vanninni">PMID:17721440</ref>. Histone Deacetylation is the reversal process for this acetylation modification. There are different classes of HDACs based on phylogenetic analysis:<br />
<br />
•Class I - HDACs 1-3 and 8, which are homologous to yeast Rpd3<br />
<br />
•Class II - HDACs 4-7, 9 and 10, which are homologous to yeast Hda1<br />
<br />
•Class III - Sirtuin deacetylases <br />
<br />
•Class IV - HDAC 11 <ref name="Vanninni" />.<br />
<br />
HDACs 1-11 are metalloenzymes and require a zinc ion for deacetylation <ref name="Vanninni" />. <br />
<br />
====HDAC8====<br />
[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.<br />
<br />
<br />
<br />
<br />
==Structure==<br />
<br />
===General Structure Information===<br />
<br />
===Inhibitor===<br />
<br />
===Potassium Binding Site===<br />
<scene name='81/812841/Potassium_binding_site/1'>Potassium Binding Site</scene><br />
==Deacetylation==<br />
<br />
===Zn<sup>2+</sup> Metal Ion Mechanism===<br />
[[Image:Hdac mech.PNG|400 px|left|thumb|Figure 1. Mechanism of HDAC8]]<br />
<br />
===Active Site===<br />
<br />
==Disease==<br />
[https://friedreichsataxianews.com/friedreichs-ataxia-experimental-treatments/histone-deacetylase-inhibitors/ HDACis]<br />
<br />
<br />
</StructureSection><br />
== References ==<br />
<references/><br />
==Student Contributors==<br />
*Cassandra Marsh<br />
*Courtney Brown<br />
*Carolyn Hurdle</div>Cassandra Marshhttps://proteopedia.org/index.php?title=User:Cassandra_Marsh/Sandbox_2&diff=3022734User:Cassandra Marsh/Sandbox 22019-04-06T18:46:50Z<p>Cassandra Marsh: </p>
<hr />
<div>=Histone Deacetylase 8 (HDAC 8), ''H. sapiens''=<br />
<StructureSection load='2v5w' size='350' frame='true' side='right' caption='HDAC 8 (PDB:2v5w)' scene=''><br />
<br />
<br />
==Introduction==<br />
===Histones===<br />
[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" />. <br />
<br />
===Histone Deacetylases (HDACs)===<br />
ε-Amino-lysine acetylation is a type of histone modification that controls the stability of proteins and biological function in eukaryotic cells <ref name="Vanninni">PMID:17721440</ref>. Histone Deacetylation is the reversal process for this acetylation modification. There are different classes of HDACs based on phylogenetic analysis:<br />
<br />
•Class I - HDACs 1-3 and 8, which are homologous to yeast Rpd3<br />
<br />
•Class II - HDACs 4-7, 9 and 10, which are homologous to yeast Hda1<br />
<br />
•Class III - Sirtuin deacetylases <br />
<br />
•Class IV - HDAC 11 <ref name="Vanninni" />.<br />
<br />
HDACs 1-11 are metalloenzymes and require a zinc ion for deacetylation <ref name="Vanninni" />. <br />
<br />
====HDAC8====<br />
[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.<br />
<br />
<br />
<br />
<br />
==Structure==<br />
<br />
===General Structure Information===<br />
<br />
===Inhibitor===<br />
<br />
===Potassium Binding Site===<br />
<br />
==Deacetylation==<br />
<br />
===Zn<sup>2+</sup> Metal Ion Mechanism===<br />
[[Image:Hdac mech.PNG|400 px|left|thumb|Figure 1. Mechanism of HDAC8]]<br />
<br />
===Active Site===<br />
<br />
==Disease==<br />
[https://friedreichsataxianews.com/friedreichs-ataxia-experimental-treatments/histone-deacetylase-inhibitors/ HDACis]<br />
<br />
<br />
</StructureSection><br />
== References ==<br />
<references/><br />
==Student Contributors==<br />
*Cassandra Marsh<br />
*Courtney Brown<br />
*Carolyn Hurdle</div>Cassandra Marshhttps://proteopedia.org/index.php?title=User:Cassandra_Marsh/Sandbox_2&diff=3022733User:Cassandra Marsh/Sandbox 22019-04-06T18:43:57Z<p>Cassandra Marsh: </p>
<hr />
<div>=Histone Deacetylase 8 (HDAC 8), ''H. sapiens''=<br />
<StructureSection load='2v5w' size='350' frame='true' side='right' caption='HDAC 8 (PDB:2v5w)' scene=''><br />
<br />
<br />
==Introduction==<br />
===Histones===<br />
[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" />. <br />
<br />
===Histone Deacetylases (HDACs)===<br />
ε-Amino-lysine acetylation is a type of histone modification that controls the stability of proteins and biological function in eukaryotic cells <ref name="Vanninni">PMID:17721440</ref>. Histone Deacetylation is the reversal process for this acetylation modification. There are different classes of HDACs based on phylogenetic analysis:<br />
<br />
•Class I - HDACs 1-3 and 8, which are homologous to yeast Rpd3<br />
<br />
•Class II - HDACs 4-7, 9 and 10, which are homologous to yeast Hda1<br />
<br />
•Class III - Sirtuin deacetylases <br />
<br />
•Class IV - HDAC 11 <ref name="Vanninni" />.<br />
<br />
HDACs 1-11 are metalloenzymes and require a zinc ion for deacetylation <ref name="Vanninni" />. <br />
<br />
====HDAC8====<br />
[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.<br />
<br />
<br />
<br />
<br />
==Structure==<br />
<br />
===General Structure Information===<br />
<br />
===Inhibitor===<br />
<br />
===Potassium Binding Site===<br />
<br />
==Deacetylation==<br />
<br />
===Zn<sup>2+</sup> Metal Ion Mechanism===<br />
[[Image:Hdac mech.PNG|400 px|left|thumb|Figure 1. Mechanism of HDAC8]]<br />
<br />
===Active Site===<br />
<br />
==Disease==<br />
[https://friedreichsataxianews.com/friedreichs-ataxia-experimental-treatments/histone-deacetylase-inhibitors/ HDACis]<br />
<br />
<br />
</StructureSection><br />
== References ==<br />
<references/><br />
==Student Contributors==<br />
*Cassandra Marsh<br />
*Courtney Brown<br />
*Carolyn Hurdle</div>Cassandra Marshhttps://proteopedia.org/index.php?title=User:Cassandra_Marsh/Sandbox_2&diff=3022732User:Cassandra Marsh/Sandbox 22019-04-06T18:33:09Z<p>Cassandra Marsh: </p>
<hr />
<div>=Histone Deacetylase 8 (HDAC 8), ''H. sapiens''=<br />
<StructureSection load='2v5w' size='350' frame='true' side='right' caption='HDAC 8 (PDB:2v5w)' scene=''><br />
<br />
<br />
==Introduction==<br />
===Histones===<br />
[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" />. <br />
<br />
===Histone Deacetylases (HDACs)===<br />
ε-Amino-lysine acetylation is a type of histone modification that controls the stability of proteins and biological function in eukaryotic cells <ref name="Vanninni">PMID:17721440</ref>. Histone Deacetylation is the reversal process for this acetylation modification. There are different classes of HDACs based on phylogenetic analysis:<br />
<br />
•Class I - HDACs 1-3 and 8, which are homologous to yeast Rpd3<br />
<br />
•Class II - HDACs 4-7, 9 and 10, which are homologous to yeast Hda1<br />
<br />
•Class III - Sirtuin deacetylases <br />
<br />
•Class IV - HDAC 11 <ref name="Vanninni" />.<br />
<br />
HDACs 1-11 are metalloenzymes and require a zinc ion for deacetylation <ref name="Vanninni" />. <br />
<br />
====HDAC8====<br />
[https://en.wikipedia.org/wiki/HDAC8 Histone Deacetylase 8] is an enzyme found in ''[https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]''. <br />
<br />
<br />
==Structure==<br />
<br />
===General Structure Information===<br />
<br />
===Inhibitor===<br />
<br />
===Potassium Binding Site===<br />
<br />
==Deacetylation==<br />
<br />
===Zn<sup>2+</sup> Metal Ion Mechanism===<br />
[[Image:Hdac mech.PNG|400 px|left|thumb|Figure 1. Mechanism of HDAC8]]<br />
<br />
===Active Site===<br />
<br />
==Disease==<br />
[https://friedreichsataxianews.com/friedreichs-ataxia-experimental-treatments/histone-deacetylase-inhibitors/ HDACis]<br />
<br />
<br />
</StructureSection><br />
== References ==<br />
<references/><br />
==Student Contributors==<br />
*Cassandra Marsh<br />
*Courtney Brown<br />
*Carolyn Hurdle</div>Cassandra Marshhttps://proteopedia.org/index.php?title=User:Cassandra_Marsh/Sandbox_2&diff=3022731User:Cassandra Marsh/Sandbox 22019-04-06T18:27:16Z<p>Cassandra Marsh: </p>
<hr />
<div>=Histone Deacetylase 8 (HDAC 8), ''H. sapians''=<br />
<StructureSection load='2v5w' size='350' frame='true' side='right' caption='HDAC 8 (PDB:2v5w)' scene=''><br />
<br />
<br />
==Introduction==<br />
===Histones===<br />
[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" />. <br />
<br />
===Histone Deacetylases (HDACs)===<br />
ε-Amino-lysine acetylation is a type of histone modification that controls the stability of proteins and biological function in eukaryotic cells <ref name="Vanninni">PMID:17721440</ref>. Histone Deacetylation is the reversal process for this acetylation modification. There are different classes of HDACs based on phylogenetic analysis:<br />
<br />
•Class I - HDACs 1-3 and 8, which are homologous to yeast Rpd3<br />
<br />
•Class II - HDACs 4-7, 9 and 10, which are homologous to yeast Hda1<br />
<br />
•Class III - Sirtuin deacetylases <br />
<br />
•Class IV - HDAC 11 <ref name="Vanninni" />.<br />
<br />
HDACs 1-11 are metalloenzymes and require a zinc ion for deacetylation <ref name="Vanninni" />. <br />
<br />
====HDAC8====<br />
[https://en.wikipedia.org/wiki/HDAC8 Histone Deacetylase 8] is <br />
<br />
<br />
==Structure==<br />
<br />
===General Structure Information===<br />
<br />
===Inhibitor===<br />
<br />
===Potassium Binding Site===<br />
<br />
==Deacetylation==<br />
<br />
===Zn<sup>2+</sup> Metal Ion Mechanism===<br />
[[Image:Hdac mech.PNG|400 px|left|thumb|Figure 1. Mechanism of HDAC8]]<br />
<br />
===Active Site===<br />
<br />
==Disease==<br />
[https://friedreichsataxianews.com/friedreichs-ataxia-experimental-treatments/histone-deacetylase-inhibitors/ HDACis]<br />
<br />
<br />
</StructureSection><br />
== References ==<br />
<references/><br />
==Student Contributors==<br />
*Cassandra Marsh<br />
*Courtney Brown<br />
*Carolyn Hurdle</div>Cassandra Marshhttps://proteopedia.org/index.php?title=User:Cassandra_Marsh/Sandbox_2&diff=3022730User:Cassandra Marsh/Sandbox 22019-04-06T18:17:55Z<p>Cassandra Marsh: </p>
<hr />
<div>=Histone Deacetylase 8 (HDAC 8), ''H. sapians''=<br />
<StructureSection load='2v5w' size='350' frame='true' side='right' caption='HDAC 8 (PDB:2v5w)' scene=''><br />
<br />
<br />
==Introduction==<br />
===Histones===<br />
[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" />. 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" />. <br />
<br />
===Histone Deacetylases (HDACs)===<br />
ε-Amino-lysine acetylation is a type of histone modification that controls the stability of proteins and biological function in eukaryotic cells <ref name="Vanninni">PMID:17721440</ref>. Histone Deacetylation is the reversal process for this acetylation modification. There are different classes of HDACs based on phylogenetic analysis:<br />
<br />
•Class I - HDACs 1-3 and 8, which are homologous to yeast Rpd3<br />
<br />
•Class II - HDACs 4-7, 9 and 10, which are homologous to yeast Hda1<br />
<br />
•Class III - Sirtuin deacetylases <br />
<br />
•Class IV - HDAC 11 <ref name="Vanninni" />.<br />
<br />
HDACs 1-11 are metalloenzymes and require a zinc ion for deacetylation <ref name="Vanninni" />. <br />
<br />
====HDAC8====<br />
[https://en.wikipedia.org/wiki/HDAC8 Histone Deacetylase 8] is <br />
<br />
<br />
==Structure==<br />
<br />
===General Structure Information===<br />
<br />
===Inhibitor===<br />
<br />
===Potassium Binding Site===<br />
<br />
==Deacetylation==<br />
<br />
===Zn<sup>2+</sup> Metal Ion Mechanism===<br />
[[Image:Hdac mech.PNG|400 px|left|thumb|Figure 1. Mechanism of HDAC8]]<br />
<br />
===Active Site===<br />
<br />
==Disease==<br />
[https://friedreichsataxianews.com/friedreichs-ataxia-experimental-treatments/histone-deacetylase-inhibitors/ HDACis]<br />
<br />
<br />
</StructureSection><br />
== References ==<br />
<references/><br />
==Student Contributors==<br />
*Cassandra Marsh<br />
*Courtney Brown<br />
*Carolyn Hurdle</div>Cassandra Marshhttps://proteopedia.org/index.php?title=User:Cassandra_Marsh/Sandbox_2&diff=3022729User:Cassandra Marsh/Sandbox 22019-04-06T18:10:05Z<p>Cassandra Marsh: </p>
<hr />
<div>=Histone Deacetylase 8 (HDAC 8), ''H. sapians''=<br />
<StructureSection load='2v5w' size='350' frame='true' side='right' caption='HDAC 8 (PDB:2v5w)' scene=''><br />
<br />
<br />
==Introduction==<br />
===Histones===<br />
[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" />. 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" />. <br />
<br />
===Histone Deacetylases (HDACs)===<br />
ε-Amino-lysine acetylation is a type of histone modification that controls the stability of proteins and biological function in eukaryotic cells <ref name="Vanninni">doi::10.1038/sj.embor.7401047</ref>. Histone Deacetylation is the reversal process for this acetylation modification. There are different classes of HDACs based on phylogenetic analysis:<br />
<br />
•Class I - HDACs 1-3 and 8, which are homologous to yeast Rpd3<br />
<br />
•Class II - HDACs 4-7, 9 and 10, which are homologous to yeast Hda1<br />
<br />
•Class III - Sirtuin deacetylases <br />
<br />
•Class IV - HDAC 11 <ref name="Vanninni" />.<br />
<br />
HDACs 1-11 are metalloenzymes and require a zinc ion for deacetylation <ref name="Vanninni" />. <br />
<br />
====HDAC8====<br />
[https://en.wikipedia.org/wiki/HDAC8 Histone Deacetylase 8] is <br />
<br />
<br />
==Structure==<br />
<br />
===General Structure Information===<br />
<br />
===Inhibitor===<br />
<br />
===Potassium Binding Site===<br />
<br />
==Deacetylation==<br />
<br />
===Zn<sup>2+</sup> Metal Ion Mechanism===<br />
[[Image:Hdac mech.PNG|400 px|left|thumb|Figure 1. Mechanism of HDAC8]]<br />
<br />
===Active Site===<br />
<br />
==Disease==<br />
[https://friedreichsataxianews.com/friedreichs-ataxia-experimental-treatments/histone-deacetylase-inhibitors/ HDACis]<br />
<br />
<br />
</StructureSection><br />
== References ==<br />
<references/><br />
==Student Contributors==<br />
*Cassandra Marsh<br />
*Courtney Brown<br />
*Carolyn Hurdle</div>Cassandra Marshhttps://proteopedia.org/index.php?title=User:Cassandra_Marsh/Sandbox_2&diff=3022728User:Cassandra Marsh/Sandbox 22019-04-06T18:02:44Z<p>Cassandra Marsh: New page: =Histone Deacetylase 8 (HDAC 8), ''H. sapians''= <StructureSection load='2v5w' size='350' frame='true' side='right' caption='HDAC 8 (PDB:2v5w)' scene=''> ==Introduction== ===Histones=== ...</p>
<hr />
<div>=Histone Deacetylase 8 (HDAC 8), ''H. sapians''=<br />
<StructureSection load='2v5w' size='350' frame='true' side='right' caption='HDAC 8 (PDB:2v5w)' scene=''><br />
<br />
<br />
==Introduction==<br />
===Histones===<br />
[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" />. 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" />. <br />
<br />
===Histone Deacetylases (HDACs)===<br />
ε-Amino-lysine acetylation is a type of histone modification that controls the stability of proteins and biological function in eukaryotic cells <ref name="Vanninni">doi:10.1038/sj.embor.7401047</ref>. Histone Deacetylation is the reversal process for this acetylation modification. There are different classes of HDACs based on phylogenetic analysis:<br />
<br />
•Class I - HDACs 1-3 and 8, which are homologous to yeast Rpd3<br />
<br />
•Class II - HDACs 4-7, 9 and 10, which are homologous to yeast Hda1<br />
<br />
•Class III - Sirtuin deacetylases <br />
<br />
•Class IV - HDAC 11 <ref name="Vanninni" />.<br />
<br />
HDACs 1-11 are metalloenzymes and require a zinc ion for deacetylation <ref name="Vanninni" />. <br />
<br />
====HDAC8====<br />
[https://en.wikipedia.org/wiki/HDAC8 Histone Deacetylase 8] is <br />
<br />
<br />
==Structure==<br />
<br />
===General Structure Information===<br />
<br />
===Inhibitor===<br />
<br />
===Potassium Binding Site===<br />
<br />
==Deacetylation==<br />
<br />
===Zn<sup>2+</sup> Metal Ion Mechanism===<br />
[[Image:Hdac mech.PNG|400 px|left|thumb|Figure 1. Mechanism of HDAC8]]<br />
<br />
===Active Site===<br />
<br />
==Disease==<br />
[https://friedreichsataxianews.com/friedreichs-ataxia-experimental-treatments/histone-deacetylase-inhibitors/ HDACis]<br />
<br />
<br />
</StructureSection><br />
== References ==<br />
<references/><br />
==Student Contributors==<br />
*Cassandra Marsh<br />
*Courtney Brown<br />
*Carolyn Hurdle</div>Cassandra Marshhttps://proteopedia.org/index.php?title=User:Cassandra_Marsh&diff=3022727User:Cassandra Marsh2019-04-06T18:02:09Z<p>Cassandra Marsh: </p>
<hr />
<div>*[[User:Cassandra Marsh/Sandbox 1]]<br />
*[[User:Cassandra Marsh/Sandbox 2]]<br />
* Full Real Name: Cassandra Marsh<br />
<br />
* Position: Student<br />
<br />
* Institution (NO ABBREVIATIONS): Butler University<br />
<br />
* City, State/Province, Country: Indianapolis, IN 46208<br />
<br />
* Field of Expertise or Study: Chemistry</div>Cassandra Marshhttps://proteopedia.org/index.php?title=User:Cassandra_Marsh/Sandbox_1&diff=3022726User:Cassandra Marsh/Sandbox 12019-04-06T17:52:51Z<p>Cassandra Marsh: </p>
<hr />
<div>=Histone Deacetylase 8 (HDAC 8), ''H. sapians''=<br />
<StructureSection load='2v5w' size='350' frame='true' side='right' caption='HDAC 8 (PDB:2v5w)' scene=''><br />
<br />
<br />
==Introduction==<br />
===Histones===<br />
[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" />. 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" />. <br />
<br />
===Histone Deacetylases (HDACs)===<br />
ε-Amino-lysine acetylation is a type of histone modification that controls the stability of proteins and biological function in eukaryotic cells <ref name="Vanninni">doi:10.1038/sj.embor.7401047</ref>. Histone Deacetylation is the reversal process for this acetylation modification. There are different classes of HDACs based on phylogenetic analysis:<br />
<br />
•Class I - HDACs 1-3 and 8, which are homologous to yeast Rpd3<br />
<br />
•Class II - HDACs 4-7, 9 and 10, which are homologous to yeast Hda1<br />
<br />
•Class III - Sirtuin deacetylases <br />
<br />
•Class IV - HDAC 11 <ref name="Vanninni" />.<br />
<br />
HDACs 1-11 are metalloenzymes and require a zinc ion for deacetylation <ref name="Vanninni" />. <br />
<br />
====HDAC8====<br />
[https://en.wikipedia.org/wiki/HDAC8 Histone Deacetylase 8] is <br />
<br />
<br />
==Structure==<br />
<br />
===General Structure Information===<br />
<br />
===Inhibitor===<br />
<br />
===Potassium Binding Site===<br />
<br />
==Deacetylation==<br />
<br />
===Zn<sup>2+</sup> Metal Ion Mechanism===<br />
[[Image:Hdac mech.PNG|400 px|left|thumb|Figure 1. Mechanism of HDAC8]]<br />
<br />
===Active Site===<br />
<br />
==Disease==<br />
[https://friedreichsataxianews.com/friedreichs-ataxia-experimental-treatments/histone-deacetylase-inhibitors/ HDACis]<br />
<br />
<br />
</StructureSection><br />
== References ==<br />
<references/><br />
==Student Contributors==<br />
*Cassandra Marsh<br />
*Courtney Brown<br />
*Carolyn Hurdle</div>Cassandra Marshhttps://proteopedia.org/index.php?title=User:Cassandra_Marsh/Sandbox_1&diff=3022725User:Cassandra Marsh/Sandbox 12019-04-06T16:43:43Z<p>Cassandra Marsh: </p>
<hr />
<div>=Histone Deacetylase 8 (HDAC 8), ''H. sapians''=<br />
<StructureSection load='2v5w' size='350' frame='true' side='right' caption='HDAC 8 (PDB:2v5w)' scene=''><br />
<br />
<br />
==Introduction==<br />
===Histones===<br />
[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" />. 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" />. <br />
<br />
===Histone Deacetylases (HDACs)===<br />
ε-Amino-lysine acetylation is a type of histone modification that controls the stability of proteins and biological function in eukaryotic cells <ref name="Vanninni">doi: :10.1038/sj.embor.7401047</ref>. Histone Deacetylation is the reversal process for this acetylation modification. There are different classes of HDACs based on phylogenetic analysis:<br />
<br />
•Class I - HDACs 1-3 and 8, which are homologous to yeast Rpd3<br />
<br />
•Class II - HDACs 4-7, 9 and 10, which are homologous to yeast Hda1<br />
<br />
•Class III - Sirtuin deacetylases <br />
<br />
•Class IV - HDAC 11 <ref name="Vanninni" />.<br />
<br />
HDACs 1-11 are metalloenzymes and require a zinc ion for deacetylation <ref name="Vanninni" />. <br />
<br />
====HDAC8====<br />
[https://en.wikipedia.org/wiki/HDAC8 Histone Deacetylase 8] is <br />
<br />
<br />
==Structure==<br />
<br />
===General Structure Information===<br />
<br />
===Inhibitor===<br />
<br />
===Potassium Binding Site===<br />
<br />
==Deacetylation==<br />
<br />
===Zn<sup>2+</sup> Metal Ion Mechanism===<br />
[[Image:Hdac mech.PNG|400 px|left|thumb|Figure 1. Mechanism of HDAC8]]<br />
<br />
===Active Site===<br />
<br />
==Disease==<br />
[https://friedreichsataxianews.com/friedreichs-ataxia-experimental-treatments/histone-deacetylase-inhibitors/ HDACis]<br />
<br />
<br />
</StructureSection><br />
== References ==<br />
<references/><br />
==Student Contributors==<br />
*Cassandra Marsh<br />
*Courtney Brown<br />
*Carolyn Hurdle</div>Cassandra Marshhttps://proteopedia.org/index.php?title=User:Cassandra_Marsh/Sandbox_1&diff=3022712User:Cassandra Marsh/Sandbox 12019-04-05T18:42:00Z<p>Cassandra Marsh: </p>
<hr />
<div>=Histone Deacetylase 8 (HDAC 8), ''H. sapians''=<br />
<StructureSection load='2v5w' size='350' frame='true' side='right' caption='HDAC 8 (PDB:2v5w)' scene=''><br />
<br />
<br />
==Introduction==<br />
===Histones===<br />
[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" />. 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" />. <br />
<br />
===Histone Deacetylases (HDACs)===<br />
ε-Amino-lysine acetylation is a type of modification that controls the stability of proteins and biological function in eukaryotic cells <ref name="Vanninni" />. There are different classes of HDACs based on phylogenetic analysis:<br />
<br />
•Class I - HDACs 1-3 and 8, which are homologous to yeast Rpd3<br />
<br />
•Class II - HDACs 4-7, 9 and 10, which are homologous to yeast Hda1 <ref name="Vanninni">doi: :10.1038/sj.embor.7401047</ref>.<br />
<br />
HDACs 1-11 are metalloenzymes and require a zinc ion for deacetylation <ref name="Vanninni" />. <br />
<br />
====HDAC8====<br />
[https://en.wikipedia.org/wiki/HDAC8 Histone Deacetylase 8] is <br />
<br />
<br />
==Structure==<br />
<br />
===General Structure Information===<br />
<br />
===Inhibitor===<br />
<br />
===Potassium Binding Site===<br />
<br />
==Deacetylation==<br />
<br />
===Zn<sup>2+</sup> Metal Ion Mechanism===<br />
[[Image:Hdac mech.PNG|400 px|left|thumb|Figure 1. Mechanism of HDAC8]]<br />
<br />
===Active Site===<br />
<br />
==Disease==<br />
[https://friedreichsataxianews.com/friedreichs-ataxia-experimental-treatments/histone-deacetylase-inhibitors/ HDACis]<br />
<br />
<br />
</StructureSection><br />
== References ==<br />
<references/><br />
==Student Contributors==<br />
*Cassandra Marsh<br />
*Courtney Brown<br />
*Carolyn Hurdle</div>Cassandra Marshhttps://proteopedia.org/index.php?title=User:Cassandra_Marsh/Sandbox_1&diff=3022686User:Cassandra Marsh/Sandbox 12019-04-05T18:19:13Z<p>Cassandra Marsh: </p>
<hr />
<div>=Histone Deacetylase 8 (HDAC 8), ''H. sapians''=<br />
<StructureSection load='2v5w' size='350' frame='true' side='right' caption='HDAC 8 (PDB:2v5w)' scene=''><br />
<br />
<br />
==Introduction==<br />
===Histones===<br />
[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" />. 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" />. <br />
<br />
<br />
===HDAC8===<br />
[https://en.wikipedia.org/wiki/HDAC8 Histone Deacetylase 8] is <br />
<br />
<br />
==Structure==<br />
<br />
===General Structure Information===<br />
<br />
===Inhibitor===<br />
<br />
===Potassium Binding Site===<br />
<br />
==Deacetylation==<br />
<br />
===Zn<sup>2+</sup> Metal Ion Mechanism===<br />
[[Image:Hdac mech.PNG|400 px|left|thumb|Figure 1. Mechanism of HDAC8]]<br />
<br />
===Active Site===<br />
<br />
==Disease==<br />
[https://friedreichsataxianews.com/friedreichs-ataxia-experimental-treatments/histone-deacetylase-inhibitors/ HDACis]<br />
<br />
<br />
</StructureSection><br />
== References ==<br />
<references/><br />
==Student Contributors==<br />
*Cassandra Marsh<br />
*Courtney Brown<br />
*Carolyn Hurdle</div>Cassandra Marshhttps://proteopedia.org/index.php?title=User:Cassandra_Marsh/Sandbox_1&diff=3022678User:Cassandra Marsh/Sandbox 12019-04-05T18:09:02Z<p>Cassandra Marsh: </p>
<hr />
<div>=Histone Deacetylase 8 (HDAC 8), ''H. sapians''=<br />
<StructureSection load='2v5w' size='350' frame='true' side='right' caption='HDAC 8 (PDB:2v5w)' scene=''><br />
<br />
<br />
==Introduction==<br />
===Histones===<br />
[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" />. Each histone octamer is made up of two copies of four different histone proteins, [https://en.wikipedia.org/wiki/Histone_H2A H2A], [https://en.wikipedia.org/wiki/Histone_H2B H2B], [https://en.wikipedia.org/wiki/Histone_H3 H3] and [https://en.wikipedia.org/wiki/Histone_H4 H4] <ref name="Histones" />. There are 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" />.<br />
<br />
<br />
===HDAC8===<br />
[https://en.wikipedia.org/wiki/HDAC8 Histone Deacetylase 8] is <br />
<br />
<br />
==Structure==<br />
<br />
===General Structure Information===<br />
<br />
===Inhibitor===<br />
<br />
===Potassium Binding Site===<br />
<br />
==Deacetylation==<br />
<br />
===Zn<sup>2+</sup> Metal Ion Mechanism===<br />
[[Image:Hdac mech.PNG|400 px|left|thumb|Figure 1. Mechanism of HDAC8]]<br />
<br />
===Active Site===<br />
<br />
==Disease==<br />
[https://friedreichsataxianews.com/friedreichs-ataxia-experimental-treatments/histone-deacetylase-inhibitors/ HDACis]<br />
<br />
<br />
</StructureSection><br />
== References ==<br />
<references/><br />
==Student Contributors==<br />
*Cassandra Marsh<br />
*Courtney Brown<br />
*Carolyn Hurdle</div>Cassandra Marshhttps://proteopedia.org/index.php?title=User:Cassandra_Marsh/Sandbox_1&diff=3022674User:Cassandra Marsh/Sandbox 12019-04-05T18:05:33Z<p>Cassandra Marsh: </p>
<hr />
<div>=Histone Deacetylase 8 (HDAC 8), ''H. sapians''=<br />
<StructureSection load='2v5w' size='350' frame='true' side='right' caption='HDAC 8 (PDB:2v5w)' scene=''><br />
<br />
<br />
==Introduction==<br />
===Histones===<br />
[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" />. Each histone octamer is made up of two copies of four different histone proteins, [https://en.wikipedia.org/wiki/Histone_H2A H2A], [https://en.wikipedia.org/wiki/Histone_H2B H2B], [https://en.wikipedia.org/wiki/Histone_H3 H3] and [https://en.wikipedia.org/wiki/Histone_H4 H4] <ref name="Histones" />. <br />
<br />
<br />
There are 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" />.<br />
<br />
<br />
===HDAC8===<br />
[https://en.wikipedia.org/wiki/HDAC8 Histone Deacetylase 8]<br />
<br />
<br />
==Structure==<br />
<br />
===General Structure Information===<br />
<br />
===Inhibitor===<br />
<br />
===Potassium Binding Site===<br />
<br />
==Deacetylation==<br />
<br />
===Zn<sup>2+</sup> Metal Ion Mechanism===<br />
[[Image:Hdac mech.PNG|400 px|left|thumb|Figure 1. Mechanism of HDAC8]]<br />
<br />
===Active Site===<br />
<br />
==Disease==<br />
[https://friedreichsataxianews.com/friedreichs-ataxia-experimental-treatments/histone-deacetylase-inhibitors/ HDACis]<br />
<br />
<br />
</StructureSection><br />
== References ==<br />
<references/><br />
==Student Contributors==<br />
*Cassandra Marsh<br />
*Courtney Brown<br />
*Carolyn Hurdle</div>Cassandra Marshhttps://proteopedia.org/index.php?title=User:Cassandra_Marsh/Sandbox_1&diff=3022663User:Cassandra Marsh/Sandbox 12019-04-05T17:55:33Z<p>Cassandra Marsh: </p>
<hr />
<div>=Histone Deacetylase 8 (HDAC 8), ''H. sapians''=<br />
<StructureSection load='2v5w' size='350' frame='true' side='right' caption='HDAC 8 (PDB:2v5w)' scene=''><br />
<br />
<br />
==Introduction==<br />
===Histones===<br />
[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" />. Each histone octamer is made up of two copies of four different histone proteins, [https://en.wikipedia.org/wiki/Histone_H2A H2A], [https://en.wikipedia.org/wiki/Histone_H2B H2B], [https://en.wikipedia.org/wiki/Histone_H3 H3] and [https://en.wikipedia.org/wiki/Histone_H4 H4] <ref name="Histones" />. <br />
<br />
<br />
[https://en.wikipedia.org/wiki/Epigenetics Epigenetics]<br />
[https://en.wikipedia.org/wiki/Histone_deacetylase Histone Deacetylase]<br />
<br />
<br />
<br />
===HDAC8===<br />
[https://en.wikipedia.org/wiki/HDAC8 Histone Deacetylase 8]<br />
<br />
<br />
==Structure==<br />
<br />
===General Structure Information===<br />
<br />
===Inhibitor===<br />
<br />
===Potassium Binding Site===<br />
<br />
==Deacetylation==<br />
<br />
===Zn<sup>2+</sup> Metal Ion Mechanism===<br />
[[Image:Hdac mech.PNG|400 px|left|thumb|Figure 1. Mechanism of HDAC8]]<br />
<br />
===Active Site===<br />
<br />
==Disease==<br />
[https://friedreichsataxianews.com/friedreichs-ataxia-experimental-treatments/histone-deacetylase-inhibitors/ HDACis]<br />
<br />
<br />
</StructureSection><br />
== References ==<br />
<references/><br />
==Student Contributors==<br />
*Cassandra Marsh<br />
*Courtney Brown<br />
*Carolyn Hurdle</div>Cassandra Marshhttps://proteopedia.org/index.php?title=User:Cassandra_Marsh/Sandbox_1&diff=3022661User:Cassandra Marsh/Sandbox 12019-04-05T17:48:10Z<p>Cassandra Marsh: </p>
<hr />
<div>=Histone Deacetylase 8 (HDAC 8), ''H. sapians''=<br />
<StructureSection load='2v5w' size='350' frame='true' side='right' caption='HDAC 8 (PDB:2v5w)' scene=''><br />
<br />
<br />
==Introduction==<br />
[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>.<br />
<br />
<br />
[https://en.wikipedia.org/wiki/Epigenetics Epigenetics]<br />
[https://en.wikipedia.org/wiki/Histone_deacetylase Histone Deacetylase]<br />
<br />
===Histones===<br />
<br />
===HDAC8===<br />
[https://en.wikipedia.org/wiki/HDAC8 Histone Deacetylase 8]<br />
<br />
<br />
==Structure==<br />
<br />
===General Structure Information===<br />
<br />
===Inhibitor===<br />
<br />
===Potassium Binding Site===<br />
<br />
==Deacetylation==<br />
<br />
===Zn<sup>2+</sup> Metal Ion Mechanism===<br />
[[Image:Hdac mech.PNG|400 px|left|thumb|Figure 1. Mechanism of HDAC8]]<br />
<br />
===Active Site===<br />
<br />
==Disease==<br />
[https://friedreichsataxianews.com/friedreichs-ataxia-experimental-treatments/histone-deacetylase-inhibitors/ HDACis]<br />
<br />
<br />
</StructureSection><br />
== References ==<br />
<references/><br />
==Student Contributors==<br />
*Cassandra Marsh<br />
*Courtney Brown<br />
*Carolyn Hurdle</div>Cassandra Marshhttps://proteopedia.org/index.php?title=User:Cassandra_Marsh/Sandbox_1&diff=3019251User:Cassandra Marsh/Sandbox 12019-03-29T18:25:40Z<p>Cassandra Marsh: </p>
<hr />
<div>=Histone Deacetylase 8 (HDAC 8), ''H. sapians''=<br />
<StructureSection load='2v5w' size='350' frame='true' side='right' caption='HDAC 8 (PDB:2v5w)' scene=''><br />
<br />
<br />
==Introduction==<br />
[https://en.wikipedia.org/wiki/Histone Histones]<br />
[https://en.wikipedia.org/wiki/Epigenetics Epigenetics]<br />
[https://en.wikipedia.org/wiki/Histone_deacetylase Histone Deacetylase]<br />
<br />
===Histones===<br />
<br />
===HDAC8===<br />
[https://en.wikipedia.org/wiki/HDAC8 Histone Deacetylase 8]<br />
<br />
<br />
==Structure==<br />
<br />
===General Structure Information===<br />
<br />
===Inhibitor===<br />
<br />
===Potassium Binding Site===<br />
<br />
==Deacetylation==<br />
<br />
===Zn<sup>2+</sup> Metal Ion Mechanism===<br />
[[Image:Hdac mech.PNG|400 px|left|thumb|Figure 1. Mechanism of HDAC8]]<br />
<br />
===Active Site===<br />
<br />
==Disease==<br />
[https://friedreichsataxianews.com/friedreichs-ataxia-experimental-treatments/histone-deacetylase-inhibitors/ HDACis]<br />
<br />
<br />
</StructureSection><br />
== References ==<br />
<references/><br />
==Student Contributors==<br />
*Cassandra Marsh<br />
*Courtney Brown<br />
*Carolyn Hurdle</div>Cassandra Marshhttps://proteopedia.org/index.php?title=User:Cassandra_Marsh/Sandbox_1&diff=3019249User:Cassandra Marsh/Sandbox 12019-03-29T18:24:36Z<p>Cassandra Marsh: </p>
<hr />
<div>=Histone Deacetylase 8 (HDAC 8), ''H. sapians''=<br />
<StructureSection load='2v5w' size='350' frame='true' side='right' caption='HDAC 8 (PDB:2v5w)' scene=''><br />
This is a default text for your page '''Cassandra Marsh/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
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.<br />
<br />
==Introduction==<br />
[https://en.wikipedia.org/wiki/Histone Histones]<br />
[https://en.wikipedia.org/wiki/Epigenetics Epigenetics]<br />
[https://en.wikipedia.org/wiki/Histone_deacetylase Histone Deacetylase]<br />
<br />
===Histones===<br />
<br />
===HDAC8===<br />
[https://en.wikipedia.org/wiki/HDAC8 Histone Deacetylase 8]<br />
<br />
<br />
==Structure==<br />
<br />
===General Structure Information===<br />
<br />
===Inhibitor===<br />
<br />
===Potassium Binding Site===<br />
<br />
==Deacetylation==<br />
<br />
===Zn<sup>2+</sup> Metal Ion Mechanism===<br />
[[Image:Hdac mech.PNG|400 px|left|thumb|Figure 1. Mechanism of HDAC8]]<br />
<br />
===Active Site===<br />
<br />
==Disease==<br />
[https://friedreichsataxianews.com/friedreichs-ataxia-experimental-treatments/histone-deacetylase-inhibitors/ HDACis]<br />
<br />
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.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/><br />
==Student Contributors==<br />
*Cassandra Marsh<br />
*Courtney Brown<br />
*Carolyn Hurdle</div>Cassandra Marshhttps://proteopedia.org/index.php?title=User:Cassandra_Marsh/Sandbox_1&diff=3019247User:Cassandra Marsh/Sandbox 12019-03-29T18:23:31Z<p>Cassandra Marsh: </p>
<hr />
<div>=Histone Deacetylase 8 (HDAC 8), ''H. sapians''=<br />
<StructureSection load='2v5w' size='350' frame='true' side='right' caption='HDAC 8 (PDB:2v5w)' scene=''><br />
This is a default text for your page '''Cassandra Marsh/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
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.<br />
<br />
==Introduction==<br />
[https://en.wikipedia.org/wiki/Histone Histones]<br />
[https://en.wikipedia.org/wiki/Epigenetics Epigenetics]<br />
[https://en.wikipedia.org/wiki/Histone_deacetylase Histone Deacetylase]<br />
<br />
===Histones===<br />
<br />
===HDAC8===<br />
[https://en.wikipedia.org/wiki/HDAC8 Histone Deacetylase 8]<br />
<br />
<br />
==Structure==<br />
<br />
===General Structure Information===<br />
<br />
===Inhibitor===<br />
<br />
===Potassium Binding Site===<br />
<br />
==Deacetylation==<br />
<br />
===Zn<sup>2+</sup> Metal Ion Mechanism===<br />
[[Image:Hdac mech.PNG|400 px|left|thumb|Figure 1. Mechanism of HDAC8]]<br />
<br />
===Active Site===<br />
<br />
==Disease==<br />
<br />
<br />
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.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/><br />
==Student Contributors==<br />
*Cassandra Marsh<br />
*Courtney Brown<br />
*Carolyn Hurdle</div>Cassandra Marshhttps://proteopedia.org/index.php?title=User:Cassandra_Marsh/Sandbox_1&diff=3019246User:Cassandra Marsh/Sandbox 12019-03-29T18:22:25Z<p>Cassandra Marsh: </p>
<hr />
<div>=Histone Deacetylase 8 (HDAC 8), ''H. sapians''=<br />
<StructureSection load='2v5w' size='350' frame='true' side='right' caption='HDAC 8 (PDB:2v5w)' scene=''><br />
This is a default text for your page '''Cassandra Marsh/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
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.<br />
<br />
==Introduction==<br />
[https://en.wikipedia.org/wiki/Histone Histones]<br />
[https://en.wikipedia.org/wiki/Epigenetics Epigenetics]<br />
[https://en.wikipedia.org/wiki/Histone_deacetylase Histone Deacetylase]<br />
<br />
===Histones===<br />
<br />
===HDAC8===<br />
[https://en.wikipedia.org/wiki/HDAC8 Histone Deacetylase 8]<br />
<br />
<br />
==Structure==<br />
<br />
===General Structure Information===<br />
<br />
===Inhibitor===<br />
<br />
===Potassium Binding Site===<br />
<br />
==Deacetylation==<br />
<br />
===Zn<sup>2+</sup> Metal Ion Mechanism===<br />
[[Image:Hdac mech.PNG]]<br />
<br />
===Active Site===<br />
<br />
==Disease==<br />
<br />
<br />
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.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/><br />
==Student Contributors==<br />
*Cassandra Marsh<br />
*Courtney Brown<br />
*Carolyn Hurdle</div>Cassandra Marshhttps://proteopedia.org/index.php?title=File:Hdac_mech.PNG&diff=3019244File:Hdac mech.PNG2019-03-29T18:12:51Z<p>Cassandra Marsh: uploaded a new version of "Image:Hdac mech.PNG"</p>
<hr />
<div></div>Cassandra Marshhttps://proteopedia.org/index.php?title=File:Hdac_mech.PNG&diff=3019243File:Hdac mech.PNG2019-03-29T18:08:51Z<p>Cassandra Marsh: </p>
<hr />
<div></div>Cassandra Marshhttps://proteopedia.org/index.php?title=User:Cassandra_Marsh/Sandbox_1&diff=3019242User:Cassandra Marsh/Sandbox 12019-03-29T18:03:59Z<p>Cassandra Marsh: </p>
<hr />
<div>=Histone Deacetylase 8 (HDAC 8), ''H. sapians''=<br />
<StructureSection load='2v5w' size='350' frame='true' side='right' caption='HDAC 8 (PDB:2v5w)' scene=''><br />
This is a default text for your page '''Cassandra Marsh/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
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.<br />
<br />
==Introduction==<br />
[https://en.wikipedia.org/wiki/Histone Histones]<br />
[https://en.wikipedia.org/wiki/Epigenetics Epigenetics]<br />
[https://en.wikipedia.org/wiki/Histone_deacetylase Histone Deacetylase]<br />
<br />
===Histones===<br />
<br />
===HDAC8===<br />
[https://en.wikipedia.org/wiki/HDAC8 Histone Deacetylase 8]<br />
<br />
<br />
==Structure==<br />
<br />
===General Structure Information===<br />
<br />
===Inhibitor===<br />
<br />
===Potassium Binding Site===<br />
<br />
==Deacetylation==<br />
<br />
===Zn<sup>2+</sup> Metal Ion Mechanism===<br />
<br />
===Active Site===<br />
<br />
==Disease==<br />
<br />
<br />
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.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/><br />
==Student Contributors==<br />
*Cassandra Marsh<br />
*Courtney Brown<br />
*Carolyn Hurdle</div>Cassandra Marshhttps://proteopedia.org/index.php?title=User:Cassandra_Marsh/Sandbox_1&diff=3019240User:Cassandra Marsh/Sandbox 12019-03-29T17:57:49Z<p>Cassandra Marsh: </p>
<hr />
<div>=Histone Deacetylase 8 (HDAC 8), ''H. sapians''=<br />
<StructureSection load='2v5w' size='350' frame='true' side='right' caption='HDAC 8 (PDB:2v5w)' scene=''><br />
This is a default text for your page '''Cassandra Marsh/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
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.<br />
<br />
==Introduction==<br />
[https://en.wikipedia.org/wiki/Histone Histones]<br />
[https://en.wikipedia.org/wiki/Epigenetics Epigenetics]<br />
[https://en.wikipedia.org/wiki/Histone_deacetylase Histone Deacetylase]<br />
===Histones===<br />
<br />
===HDAC8===<br />
<br />
==Structure==<br />
<br />
===General Structure Information===<br />
<br />
===Inhibitor===<br />
<br />
===Potassium Binding Site===<br />
<br />
==Deacetylation==<br />
<br />
===2+ Metal Ion Mechanism===<br />
<br />
===Active Site===<br />
<br />
==Disease==<br />
<br />
<br />
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.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/><br />
==Student Contributors==<br />
*Cassandra Marsh<br />
*Courtney Brown<br />
*Carolyn Hurdle</div>Cassandra Marshhttps://proteopedia.org/index.php?title=User:Cassandra_Marsh/Sandbox_1&diff=3019239User:Cassandra Marsh/Sandbox 12019-03-29T17:51:59Z<p>Cassandra Marsh: </p>
<hr />
<div>=Histone Deacetylase 8 (HDAC 8), ''H. sapians''=<br />
<StructureSection load='2v5w' size='350' frame='true' side='right' caption='HDAC 8 (PDB:2v5w)' scene=''><br />
This is a default text for your page '''Cassandra Marsh/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
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.<br />
<br />
==Introduction==<br />
[https://en.wikipedia.org/wiki/Histone Background on Histones]<br />
[https://en.wikipedia.org/wiki/Epigenetics Epigenetics]<br />
[https://en.wikipedia.org/wiki/Histone_deacetylase Histone Deacetylase]<br />
===Histones===<br />
<br />
===Function===<br />
<scene name='81/811714/Residues_50-55/1'>Residues 50-55</scene><br />
==Inhibition==<br />
<ref name="Ransey">PMID:28504306</ref><br />
==Potassium Binding Site==<br />
<br />
[[Image:Potassium binding.png|400 px|right|thumb|Figure 1. The coolest image of this protein EVAH!!!]]<br />
==Nucleophilic Water==<br />
<ref name="Vannini">PMID:17721440</ref><br />
==Aspartate 101==<br />
<ref name="Ransey" /><br />
<br />
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.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/><br />
==Student Contributors==<br />
*Cassandra Marsh<br />
*Courtney Brown<br />
*Carolyn Hurdle</div>Cassandra Marshhttps://proteopedia.org/index.php?title=User:Cassandra_Marsh/Sandbox_1&diff=3019228User:Cassandra Marsh/Sandbox 12019-03-29T17:39:58Z<p>Cassandra Marsh: </p>
<hr />
<div>=Histone Deacetylase 8 (HDAC 8), ''H. sapians''=<br />
<StructureSection load='2v5w' size='350' frame='true' side='right' caption='HDAC 8 (PDB:2v5w)' scene=''><br />
This is a default text for your page '''Cassandra Marsh/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
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.<br />
<br />
==Introduction==<br />
[https://en.wikipedia.org/wiki/Histone Background on Histones]<br />
===Histones===<br />
<br />
===Function===<br />
<scene name='81/811714/Residues_50-55/1'>Residues 50-55</scene><br />
==Inhibition==<br />
<ref name="Ransey">PMID:28504306</ref><br />
==Potassium Binding Site==<br />
<br />
[[Image:Potassium binding.png|400 px|right|thumb|Figure 1. The coolest image of this protein EVAH!!!]]<br />
==Nucleophilic Water==<br />
<ref name="Vannini">PMID:17721440</ref><br />
==Aspartate 101==<br />
<ref name="Ransey" /><br />
<br />
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.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/><br />
==Student Contributors==<br />
*Cassandra Marsh<br />
*Courtney Brown<br />
*Carolyn Hurdle</div>Cassandra Marshhttps://proteopedia.org/index.php?title=User:Cassandra_Marsh/Sandbox_1&diff=3016430User:Cassandra Marsh/Sandbox 12019-03-22T18:27:00Z<p>Cassandra Marsh: </p>
<hr />
<div>=Histone Deacetylase 8 (HDAC 8), ''H. sapians''=<br />
<StructureSection load='2v5w' size='350' frame='true' side='right' caption='HDAC 8 (PDB:2v5w)' scene='81/811714/Residues_50-55/1'><br />
This is a default text for your page '''Cassandra Marsh/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
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.<br />
<br />
==Introduction==<br />
[https://en.wikipedia.org/wiki/Histone Background on Histones]<br />
===Histones===<br />
<br />
===Function===<br />
<scene name='81/811714/Residues_50-55/1'>Residues 50-55</scene><br />
==Inhibition==<br />
<ref name="Ransey">PMID:28504306</ref><br />
==Potassium Binding Site==<br />
<br />
[[Image:Potassium binding.png|400 px|right|thumb|Figure 1. The coolest image of this protein EVAH!!!]]<br />
==Nucleophilic Water==<br />
<ref name="Vannini">PMID:17721440</ref><br />
==Aspartate 101==<br />
<ref name="Ransey" /><br />
<br />
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.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/><br />
==Student Contributors==<br />
*Cassandra Marsh<br />
*Courtney Brown<br />
*Carolyn Hurdle</div>Cassandra Marshhttps://proteopedia.org/index.php?title=User:Cassandra_Marsh/Sandbox_1&diff=3016429User:Cassandra Marsh/Sandbox 12019-03-22T18:25:35Z<p>Cassandra Marsh: </p>
<hr />
<div>=Histone Deacetylase 8 (HDAC 8), ''H. sapians''=<br />
<StructureSection load='2v5w' size='350' frame='true' side='right' caption='HDAC 8 (PDB:2v5w)' scene=''><br />
This is a default text for your page '''Cassandra Marsh/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
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.<br />
<br />
==Introduction==<br />
[https://en.wikipedia.org/wiki/Histone Background on Histones]<br />
===Histones===<br />
<br />
===Function===<br />
<scene name='81/811714/Residues_50-55/1'>Residues 50-55</scene><br />
==Inhibition==<br />
<ref name="Ransey">PMID:28504306</ref><br />
==Potassium Binding Site==<br />
<br />
[[Image:Potassium binding.png|400 px|right|thumb|Figure 1. The coolest image of this protein EVAH!!!]]<br />
==Nucleophilic Water==<br />
<ref name="Vannini">PMID:17721440</ref><br />
==Aspartate 101==<br />
<ref name="Ransey" /><br />
<br />
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.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/><br />
==Student Contributors==<br />
*Cassandra Marsh<br />
*Courtney Brown<br />
*Carolyn Hurdle</div>Cassandra Marshhttps://proteopedia.org/index.php?title=User:Cassandra_Marsh/Sandbox_1&diff=3016383User:Cassandra Marsh/Sandbox 12019-03-22T17:58:05Z<p>Cassandra Marsh: </p>
<hr />
<div>=Histone Deacetylase 8 (HDAC 8), ''H. sapians''=<br />
<StructureSection load='2v5w' size='350' frame='true' side='right' caption='HDAC 8 (PDB:2v5w)' scene=''><br />
This is a default text for your page '''Cassandra Marsh/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
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.<br />
<br />
==Introduction==<br />
[https://en.wikipedia.org/wiki/Histone Background on Histones]<br />
===Histones===<br />
<br />
===Function===<br />
<br />
==Inhibition==<br />
<br />
==Potassium Binding Site==<br />
<br />
[[Image:Potassium binding.png|400 px|right|thumb|Figure 1. The coolest image of this protein EVAH!!!]]<br />
==Nucleophilic Water==<br />
<br />
==Aspartate 101==<br />
<br />
<br />
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.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/><br />
==Student Contributors==<br />
*Cassandra Marsh<br />
*Courtney Brown<br />
*Carolyn Hurdle</div>Cassandra Marshhttps://proteopedia.org/index.php?title=File:Potassium_binding.png&diff=3016346File:Potassium binding.png2019-03-22T17:44:32Z<p>Cassandra Marsh: uploaded a new version of "Image:Potassium binding.png": Potassium binding site for the potassium ion nearest to the active site.</p>
<hr />
<div></div>Cassandra Marshhttps://proteopedia.org/index.php?title=File:Potassium_binding.png&diff=3016323File:Potassium binding.png2019-03-22T17:40:58Z<p>Cassandra Marsh: </p>
<hr />
<div></div>Cassandra Marshhttps://proteopedia.org/index.php?title=User:Cassandra_Marsh/Sandbox_1&diff=3016305User:Cassandra Marsh/Sandbox 12019-03-22T17:34:57Z<p>Cassandra Marsh: </p>
<hr />
<div>=Histone Deacetylase 8 (HDAC 8), ''H. sapians''=<br />
<StructureSection load='2v5w' size='340' side='right' caption='HDAC 8 Structure (PDB:2v5w)' scene=''><br />
This is a default text for your page '''Cassandra Marsh/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
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.<br />
<br />
==Introduction==<br />
<br />
===Histones===<br />
<br />
===Function===<br />
<br />
==Inhibition==<br />
<br />
==Potassium Binding Site==<br />
<br />
==Nucleophilic Water==<br />
<br />
==Aspartate 101==<br />
<br />
<br />
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.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/><br />
==Student Contributors==<br />
*Cassandra Marsh<br />
*Courtney Brown<br />
*Carolyn Hurdle</div>Cassandra Marshhttps://proteopedia.org/index.php?title=User:Cassandra_Marsh/Sandbox_1&diff=3016256User:Cassandra Marsh/Sandbox 12019-03-22T17:19:01Z<p>Cassandra Marsh: New page: ==Your Heading Here (maybe something like 'Structure')== <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> This is a default text for you...</p>
<hr />
<div>==Your Heading Here (maybe something like 'Structure')==<br />
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page '''Cassandra Marsh/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br />
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.<br />
<br />
== Function ==<br />
<br />
== Disease ==<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<br />
<br />
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.<br />
<br />
</StructureSection><br />
== References ==<br />
<references/></div>Cassandra Marshhttps://proteopedia.org/index.php?title=User:Cassandra_Marsh&diff=3016248User:Cassandra Marsh2019-03-22T17:17:48Z<p>Cassandra Marsh: </p>
<hr />
<div>*[[User:Cassandra Marsh/Sandbox 1]]<br />
* Full Real Name: Cassandra Marsh<br />
<br />
* Position: Student<br />
<br />
* Institution (NO ABBREVIATIONS): Butler University<br />
<br />
* City, State/Province, Country: Indianapolis, IN 46208<br />
<br />
* Field of Expertise or Study: Chemistry</div>Cassandra Marsh