4lxz

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'''Unreleased structure'''
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{{STRUCTURE_4lxz| PDB=4lxz | SCENE= }}
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===Structure of Human HDAC2 in complex with SAHA (vorinostat)===
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{{ABSTRACT_PUBMED_23897821}}
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The entry 4lxz is ON HOLD
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==Function==
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[[http://www.uniprot.org/uniprot/HDAC2_HUMAN HDAC2_HUMAN]] Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Forms transcriptional repressor complexes by associating with MAD, SIN3, YY1 and N-COR. Interacts in the late S-phase of DNA-replication with DNMT1 in the other transcriptional repressor complex composed of DNMT1, DMAP1, PCNA, CAF1. Deacetylates TSHZ3 and regulates its transcriptional repressor activity. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development.<ref>PMID:19343227</ref>
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Authors: Fong, R., Lupardus, P.J.
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==About this Structure==
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[[4lxz]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Ochroconis_lascauxensis Ochroconis lascauxensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LXZ OCA].
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Description: Structure of Human HDAC2 in complex with SAHA (vorinostat)
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==Reference==
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<ref group="xtra">PMID:023897821</ref><references group="xtra"/><references/>
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[[Category: Histone deacetylase]]
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[[Category: Ochroconis lascauxensis]]
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[[Category: Fong, R.]]
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[[Category: Lupardus, P J.]]
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[[Category: Deacetylase]]
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[[Category: Histone]]
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[[Category: Hydrolase-hydrolase inhibitor complex]]

Revision as of 08:20, 21 August 2013

Template:STRUCTURE 4lxz

Contents

Structure of Human HDAC2 in complex with SAHA (vorinostat)

Template:ABSTRACT PUBMED 23897821

Function

[HDAC2_HUMAN] Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Forms transcriptional repressor complexes by associating with MAD, SIN3, YY1 and N-COR. Interacts in the late S-phase of DNA-replication with DNMT1 in the other transcriptional repressor complex composed of DNMT1, DMAP1, PCNA, CAF1. Deacetylates TSHZ3 and regulates its transcriptional repressor activity. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development.[1]

About this Structure

4lxz is a 3 chain structure with sequence from Ochroconis lascauxensis. Full crystallographic information is available from OCA.

Reference

  • Lauffer BE, Mintzer R, Fong R, Mukund S, Tam C, Zilberleyb I, Flicke B, Ritscher A, Fedorowicz G, Vallero R, Ortwine DF, Gunzner J, Modrusan Z, Neumann L, Koth CM, Lupardus PJ, Kaminker JS, Heise CE, Steiner P. Histone deacetylase (HDAC) inhibitor kinetic rate constants correlate with cellular histone acetylation but not transcription and cell viability. J Biol Chem. 2013 Jul 29. PMID:23897821 doi:10.1074/jbc.M113.490706
  1. ↑ Kajiwara Y, Akram A, Katsel P, Haroutunian V, Schmeidler J, Beecham G, Haines JL, Pericak-Vance MA, Buxbaum JD. FE65 binds Teashirt, inhibiting expression of the primate-specific caspase-4. PLoS One. 2009;4(4):e5071. doi: 10.1371/journal.pone.0005071. Epub 2009 Apr 3. PMID:19343227 doi:10.1371/journal.pone.0005071

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