This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


User:Cassandra Marsh/Sandbox 1

From Proteopedia

< User:Cassandra Marsh(Difference between revisions)
Jump to: navigation, search
Current revision (17:52, 6 April 2019) (edit) (undo)
 
(One intermediate revision not shown.)
Line 8: Line 8:
===Histone Deacetylases (HDACs)===
===Histone Deacetylases (HDACs)===
-
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:
+
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:
•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
-
•Class II - HDACs 4-7, 9 and 10, which are homologous to yeast Hda1 <ref name="Vanninni">doi: :10.1038/sj.embor.7401047</ref>.
+
•Class II - HDACs 4-7, 9 and 10, which are homologous to yeast Hda1
 +
 
 +
•Class III - Sirtuin deacetylases
 +
 
 +
•Class IV - HDAC 11 <ref name="Vanninni" />.
HDACs 1-11 are metalloenzymes and require a zinc ion for deacetylation <ref name="Vanninni" />.
HDACs 1-11 are metalloenzymes and require a zinc ion for deacetylation <ref name="Vanninni" />.

Current revision

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 doi: https://dx.doi.org/10.1038/sj.embor.7401047

Student Contributors

  • Cassandra Marsh
  • Courtney Brown
  • Carolyn Hurdle

Proteopedia Page Contributors and Editors (what is this?)

Cassandra Marsh

Personal tools