4lka: Difference between revisions

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{{STRUCTURE_4lka|  PDB=4lka  |  SCENE=  }}  
{{STRUCTURE_4lka|  PDB=4lka  |  SCENE=  }}  
===Crystal Structure of MOZ double PHD finger histone H3K9ac complex===
===Crystal Structure of MOZ double PHD finger histone H3K9ac complex===
{{ABSTRACT_PUBMED_24150941}}


==Disease==
==Disease==
Line 9: Line 10:


==About this Structure==
==About this Structure==
[[4lka]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LKA OCA].  
[[4lka]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LKA OCA].  


==Reference==
==Reference==
<references group="xtra"/><references/>
<ref group="xtra">PMID:024150941</ref><references group="xtra"/><references/>
[[Category: Histone acetyltransferase]]
[[Category: Histone acetyltransferase]]
[[Category: Homo sapiens]]
[[Category: Human]]
[[Category: Deeves, S E.]]
[[Category: Deeves, S E.]]
[[Category: Dreveny, I.]]
[[Category: Dreveny, I.]]

Revision as of 11:23, 5 February 2014

Template:STRUCTURE 4lka

Crystal Structure of MOZ double PHD finger histone H3K9ac complexCrystal Structure of MOZ double PHD finger histone H3K9ac complex

Template:ABSTRACT PUBMED 24150941

DiseaseDisease

[KAT6A_HUMAN] Note=Chromosomal aberrations involving KAT6A may be a cause of acute myeloid leukemias. Translocation t(8;16)(p11;p13) with CREBBP; translocation t(8;22)(p11;q13) with EP300. KAT6A-CREBBP may induce leukemia by inhibiting RUNX1-mediated transcription. Inversion inv(8)(p11;q13) generates the KAT6A-NCOA2 oncogene, which consists of the N-terminal part of KAT6A and the C-terminal part of NCOA2/TIF2. KAT6A-NCOA2 binds to CREBBP and disrupts its function in transcription activation. Note=A chromosomal aberration involving KAT6A is a cause of therapy-related myelodysplastic syndrome. Translocation t(2;8)(p23;p11.2) with ASXL2 generates a KAT6A-ASXL2 fusion protein.

FunctionFunction

[KAT6A_HUMAN] Histone acetyltransferase that acetylates lysine residues in histone H3 and histone H4 (in vitro). Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. May act as a transcriptional coactivator for RUNX1 and RUNX2.[1] [2] [3] [4] [5]

About this StructureAbout this Structure

4lka is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA.

ReferenceReference

[xtra 1]

  1. Dreveny I, Deeves SE, Fulton J, Yue B, Messmer M, Bhattacharya A, Collins HM, Heery DM. The double PHD finger domain of MOZ/MYST3 induces alpha-helical structure of the histone H3 tail to facilitate acetylation and methylation sampling and modification. Nucleic Acids Res. 2014 Jan 1;42(2):822-35. doi: 10.1093/nar/gkt931. Epub 2013, Oct 22. PMID:24150941 doi:http://dx.doi.org/10.1093/nar/gkt931
  1. Kitabayashi I, Aikawa Y, Nguyen LA, Yokoyama A, Ohki M. Activation of AML1-mediated transcription by MOZ and inhibition by the MOZ-CBP fusion protein. EMBO J. 2001 Dec 17;20(24):7184-96. PMID:11742995 doi:10.1093/emboj/20.24.7184
  2. Pelletier N, Champagne N, Stifani S, Yang XJ. MOZ and MORF histone acetyltransferases interact with the Runt-domain transcription factor Runx2. Oncogene. 2002 Apr 18;21(17):2729-40. PMID:11965546 doi:10.1038/sj.onc.1205367
  3. Bristow CA, Shore P. Transcriptional regulation of the human MIP-1alpha promoter by RUNX1 and MOZ. Nucleic Acids Res. 2003 Jun 1;31(11):2735-44. PMID:12771199
  4. Doyon Y, Cayrou C, Ullah M, Landry AJ, Cote V, Selleck W, Lane WS, Tan S, Yang XJ, Cote J. ING tumor suppressor proteins are critical regulators of chromatin acetylation required for genome expression and perpetuation. Mol Cell. 2006 Jan 6;21(1):51-64. PMID:16387653 doi:10.1016/j.molcel.2005.12.007
  5. Holbert MA, Sikorski T, Carten J, Snowflack D, Hodawadekar S, Marmorstein R. The human monocytic leukemia zinc finger histone acetyltransferase domain contains DNA-binding activity implicated in chromatin targeting. J Biol Chem. 2007 Dec 14;282(50):36603-13. Epub 2007 Oct 9. PMID:17925393 doi:10.1074/jbc.M705812200

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