3c6w: Difference between revisions

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


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==Crystal structure of the ING5 PHD finger in complex with H3K4me3 peptide==
The line below this paragraph, containing "STRUCTURE_3c6w", creates the "Structure Box" on the page.
<StructureSection load='3c6w' size='340' side='right'caption='[[3c6w]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
or leave the SCENE parameter empty for the default display.
</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>
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<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>
{{STRUCTURE_3c6w|  PDB=3c6w  |  SCENE= }}
<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>
===PHD finger of ING5 bound to an H3K4me3 peptide===
</table>
 
== Function ==
 
[[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> 
==About this Structure==
== Evolutionary Conservation ==
3C6W is a [[Protein complex]] structure of sequences 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].  
[[Image:Consurf_key_small.gif|200px|right]]
 
Check<jmol>
==Reference==
  <jmolCheckbox>
The crystal structure of the ING5 PHD finger in complex with an H3K4me3 histone peptide., Champagne KS, Saksouk N, Pena PV, Johnson K, Ullah M, Yang XJ, Cote J, Kutateladze TG, Proteins. 2008 Sep;72(4):1371-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18623064 18623064]
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c6/3c6w_consurf.spt"</scriptWhenChecked>
[[Category: Homo sapiens]]
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
[[Category: Protein complex]]
    <text>to colour the structure by Evolutionary Conservation</text>
[[Category: Champagne, K S.]]
  </jmolCheckbox>
[[Category: Johnson, K.]]
</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].
[[Category: Kutateladze, T G.]]
<div style="clear:both"></div>
[[Category: Pena, P V.]]
== 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: Alternative splicing]]
[[Category: Chromatin]]
[[Category: Chromatin]]
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[[Category: Zinc]]
[[Category: Zinc]]
[[Category: Zinc-finger]]
[[Category: Zinc-finger]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Sep 18 09:29:41 2008''

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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