3c6w: Difference between revisions

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[[Image:3c6w.png|left|200px]]


{{STRUCTURE_3c6w|  PDB=3c6w  |  SCENE=  }}
==Crystal structure of the ING5 PHD finger in complex with H3K4me3 peptide==
 
<StructureSection load='3c6w' size='340' side='right'caption='[[3c6w]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
===Crystal structure of the ING5 PHD finger in complex with H3K4me3 peptide===
== Structural highlights ==
 
<table><tr><td colspan='2'>[[3c6w]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C6W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3C6W FirstGlance]. <br>
 
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
==About this Structure==
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=M3L:N-TRIMETHYLLYSINE'>M3L</scene></td></tr>
[[3c6w]] is a 4 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=3C6W OCA].  
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ING5 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
 
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3c6w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c6w OCA], [https://pdbe.org/3c6w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3c6w RCSB], [https://www.ebi.ac.uk/pdbsum/3c6w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3c6w ProSAT]</span></td></tr>
==Reference==
</table>
<ref group="xtra">PMID:018623064</ref><references group="xtra"/>
== Function ==
[[Category: Homo sapiens]]
[[https://www.uniprot.org/uniprot/ING5_HUMAN ING5_HUMAN]] Component of the HBO1 complex which has a histone H4-specific acetyltransferase activity, a reduced activity toward histone H3 and is responsible for the bulk of histone H4 acetylation in vivo. Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. Through chromatin acetylation it may regulate DNA replication and may function as a transcriptional coactivator.<ref>PMID:12750254</ref> <ref>PMID:16387653</ref> 
[[Category: Champagne, K S.]]
== Evolutionary Conservation ==
[[Category: Johnson, K.]]
[[Image:Consurf_key_small.gif|200px|right]]
[[Category: Kutateladze, T G.]]
Check<jmol>
[[Category: Pena, P V.]]
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c6/3c6w_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3c6w ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Champagne, K S]]
[[Category: Johnson, K]]
[[Category: Kutateladze, T G]]
[[Category: Pena, P V]]
[[Category: Alternative splicing]]
[[Category: Chromatin]]
[[Category: Chromatin]]
[[Category: Epigenetic]]
[[Category: Epigenetic]]
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[[Category: Phd]]
[[Category: Phd]]
[[Category: Phosphoprotein]]
[[Category: Phosphoprotein]]
[[Category: Zinc]]
[[Category: Zinc-finger]]
[[Category: Zinc-finger]]

Latest revision as of 10:45, 27 January 2022

Crystal structure of the ING5 PHD finger in complex with H3K4me3 peptideCrystal structure of the ING5 PHD finger in complex with H3K4me3 peptide

Structural highlights

3c6w is a 4 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Gene:ING5 (HUMAN)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ING5_HUMAN] Component of the HBO1 complex which has a histone H4-specific acetyltransferase activity, a reduced activity toward histone H3 and is responsible for the bulk of histone H4 acetylation in vivo. Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. Through chromatin acetylation it may regulate DNA replication and may function as a transcriptional coactivator.[1] [2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. ↑ Shiseki M, Nagashima M, Pedeux RM, Kitahama-Shiseki M, Miura K, Okamura S, Onogi H, Higashimoto Y, Appella E, Yokota J, Harris CC. p29ING4 and p28ING5 bind to p53 and p300, and enhance p53 activity. Cancer Res. 2003 May 15;63(10):2373-8. PMID:12750254
  2. ↑ 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

3c6w, resolution 1.75Å

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