User:Asif Hossain/Sandbox 1: Difference between revisions

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==HDAC8 Structure==

The crystal structure of human HDAC8 was determined using x-ray crystallography at a 2.0Å resolution. <ref name="Vannini, A., Volpari, C., Gallinari, P.">Vannini, A., Volpari, C., Gallinari, P., Jones, P., Mattu, M., Carfí, A., ... & Di Marco, S. (2007). Substrate binding to histone deacetylases as shown by the crystal structure of the HDAC8–substrate complex. EMBO reports, 8(9), 879-884. https://doi.org/10.1038/sj.embor.7401047 </ref> The structure includes two structural K ion and one catalytic Zn ion. HDAC8 is bound to a [https://en.wikipedia.org/wiki/P53 p-53] <scene name='81/811084/Ligand/8'>derived diacetylated peptide substrate</scene> as opposed to the natural histone substrate. This peptide includes a <scene name='81/811084/Coumarin/1'>fluorescent coumarin ring</scene> likely used in past kinetic assays. The HDAC8 is made up of a <scene name='81/811084/Beta_sheets/6'>β-sheet</scene> with eight parallel β-strands located between 13 <scene name='81/811084/Alpha_helicesv2/4'>α-helices</scene>. The HDAC8 consists of 377 amino acids. <ref name="Somoza"> Somoza J, Skene R. Structural snapshots of human HDAC8 provide insights into the class I histone deacetylases. Structure, 12(7), 1325-1334.2004. https://doi.org/10.1016/j.str.2004.04.012 </ref>

The crystal structure of human HDAC8 was determined using x-ray crystallography at a 2.0Å resolution. <ref name="Vannini, A., Volpari, C., Gallinari, P.">Vannini, A., Volpari, C., Gallinari, P., Jones, P., Mattu, M., Carfí, A., ... & Di Marco, S. (2007). Substrate binding to histone deacetylases as shown by the crystal structure of the HDAC8–substrate complex. EMBO reports, 8(9), 879-884. https://doi.org/10.1038/sj.embor.7401047 </ref> The structure includes two structural K ion and one catalytic Zn ion. HDAC8 is bound to a [https://en.wikipedia.org/wiki/P53 p-53] <scene name='81/811084/Ligand/8'>derived diacetylated peptide substrate</scene> as opposed to the natural histone substrate. This peptide includes a <scene name='81/811084/Coumarin/2'>fluorescent coumarin ring</scene> likely used in past kinetic assays. The HDAC8 is made up of a <scene name='81/811084/Beta_sheets/6'>β-sheet</scene> with eight parallel β-strands located between 13 <scene name='81/811084/Alpha_helicesv2/4'>α-helices</scene>. The HDAC8 consists of 377 amino acids. <ref name="Somoza"> Somoza J, Skene R. Structural snapshots of human HDAC8 provide insights into the class I histone deacetylases. Structure, 12(7), 1325-1334.2004. https://doi.org/10.1016/j.str.2004.04.012 </ref>

===Zinc Ion===

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 ==HDAC8 Structure==
-The crystal structure of human HDAC8 was determined using x-ray crystallography at a 2.0Å resolution. <ref name="Vannini, A., Volpari, C., Gallinari, P.">Vannini, A., Volpari, C., Gallinari, P., Jones, P., Mattu, M., Carfí, A., ... & Di Marco, S. (2007). Substrate binding to histone deacetylases as shown by the crystal structure of the HDAC8–substrate complex. EMBO reports, 8(9), 879-884. https://doi.org/10.1038/sj.embor.7401047 </ref> The structure includes two structural K ion and one catalytic Zn ion. HDAC8 is bound to a [https://en.wikipedia.org/wiki/P53 p-53] <scene name='81/811084/Ligand/8'>derived diacetylated peptide substrate</scene> as opposed to the natural histone substrate. This peptide includes a <scene name='81/811084/Coumarin/1'>fluorescent coumarin ring</scene> likely used in past kinetic assays. The HDAC8 is made up of a <scene name='81/811084/Beta_sheets/6'>β-sheet</scene> with eight parallel β-strands located between 13 <scene name='81/811084/Alpha_helicesv2/4'>α-helices</scene>. The HDAC8 consists of 377 amino acids.  <ref name="Somoza"> Somoza J, Skene R. Structural snapshots of human HDAC8 provide insights into the class I histone deacetylases. Structure, 12(7), 1325-1334.2004. https://doi.org/10.1016/j.str.2004.04.012 </ref>
+The crystal structure of human HDAC8 was determined using x-ray crystallography at a 2.0Å resolution. <ref name="Vannini, A., Volpari, C., Gallinari, P.">Vannini, A., Volpari, C., Gallinari, P., Jones, P., Mattu, M., Carfí, A., ... & Di Marco, S. (2007). Substrate binding to histone deacetylases as shown by the crystal structure of the HDAC8–substrate complex. EMBO reports, 8(9), 879-884. https://doi.org/10.1038/sj.embor.7401047 </ref> The structure includes two structural K ion and one catalytic Zn ion. HDAC8 is bound to a [https://en.wikipedia.org/wiki/P53 p-53] <scene name='81/811084/Ligand/8'>derived diacetylated peptide substrate</scene> as opposed to the natural histone substrate. This peptide includes a <scene name='81/811084/Coumarin/2'>fluorescent coumarin ring</scene> likely used in past kinetic assays. The HDAC8 is made up of a <scene name='81/811084/Beta_sheets/6'>β-sheet</scene> with eight parallel β-strands located between 13 <scene name='81/811084/Alpha_helicesv2/4'>α-helices</scene>. The HDAC8 consists of 377 amino acids.  <ref name="Somoza"> Somoza J, Skene R. Structural snapshots of human HDAC8 provide insights into the class I histone deacetylases. Structure, 12(7), 1325-1334.2004. https://doi.org/10.1016/j.str.2004.04.012 </ref>
 ===Zinc Ion===