User:Cassandra Marsh/Sandbox 2

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===Histone Deacetylases (HDACs)===
===Histone Deacetylases (HDACs)===
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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:
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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:
•Class I - HDACs 1-3 and 8, which are homologous to yeast Rpd3
•Class I - HDACs 1-3 and 8, which are homologous to yeast Rpd3

Revision as of 18:17, 6 April 2019

Histone Deacetylase 8 (HDAC 8), H. sapians

HDAC 8 (PDB:2v5w)

Drag the structure with the mouse to rotate

References

  1. ↑ 1.0 1.1 1.2 Histones | Learn Science at Scitable https://www.nature.com/scitable/definition/histone-histones-57
  2. ↑ 2.0 2.1 2.2 Vannini A, Volpari C, Gallinari P, Jones P, Mattu M, Carfi A, De Francesco R, Steinkuhler C, Di Marco S. Substrate binding to histone deacetylases as shown by the crystal structure of the HDAC8-substrate complex. EMBO Rep. 2007 Sep;8(9):879-84. Epub 2007 Aug 10. PMID:17721440

Student Contributors

  • Cassandra Marsh
  • Courtney Brown
  • Carolyn Hurdle

Proteopedia Page Contributors and Editors (what is this?)

Cassandra Marsh

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