2k1j: Difference between revisions

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[[Image:2k1j.png|left|200px]]


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==Plan homeodomain finger of tumour supressor ING4==
The line below this paragraph, containing "STRUCTURE_2k1j", creates the "Structure Box" on the page.
<StructureSection load='2k1j' size='340' side='right'caption='[[2k1j]]' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2k1j]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2jmq 2jmq]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K1J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K1J FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<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>
{{STRUCTURE_2k1j|  PDB=2k1j  |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2k1j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k1j OCA], [https://pdbe.org/2k1j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k1j RCSB], [https://www.ebi.ac.uk/pdbsum/2k1j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k1j ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ING4_HUMAN ING4_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. Through chromatin acetylation it may function in DNA replication. May inhibit tumor progression by modulating the transcriptional output of signaling pathways which regulate cell proliferation. Can suppress brain tumor angiogenesis through transcriptional repression of RELA/NFKB3 target genes when complexed with RELA. May also specifically suppress loss of contact inhibition elicited by activated oncogenes such as MYC. Represses hypoxia inducible factor's (HIF) activity by interacting with HIF prolyl hydroxylase 2 (EGLN1).<ref>PMID:12750254</ref> <ref>PMID:15251430</ref> <ref>PMID:15029197</ref> <ref>PMID:15528276</ref> <ref>PMID:15897452</ref> <ref>PMID:16387653</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k1/2k1j_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=2k1j ConSurf].
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== Publication Abstract from PubMed ==
Plant homeodomain (PHD) fingers are frequently present in proteins involved in chromatin remodelling, and some of them bind to histones. The family of proteins inhibitors of growth (ING) contains a PHD finger that bind to histone-3 trimethylated at lysine 4, and those of ING1 and ING2 also act as nuclear phosphoinositide receptors. We have determined the structure of ING4 PHD, and characterised its binding to phosphoinositides and histone methylated tails. In contrast to ING2, ING4 is not a phosphoinositide receptor and binds with similar affinity to the different methylation states of histone-3 at lysine 4.


===Plan homeodomain finger of tumour supressor ING4===
Solution structure and NMR characterization of the binding to methylated histone tails of the plant homeodomain finger of the tumour suppressor ING4.,Palacios A, Garcia P, Padro D, Lopez-Hernandez E, Martin I, Blanco FJ FEBS Lett. 2006 Dec 22;580(30):6903-8. Epub 2006 Nov 30. PMID:17157298<ref>PMID:17157298</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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(as it appears on PubMed at http://www.pubmed.gov), where 17157298 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_17157298}}
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</StructureSection>
==About this Structure==
2K1J is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2jmq 2jmq]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K1J OCA].
 
==Reference==
Solution structure and NMR characterization of the binding to methylated histone tails of the plant homeodomain finger of the tumour suppressor ING4., Palacios A, Garcia P, Padro D, Lopez-Hernandez E, Martin I, Blanco FJ, FEBS Lett. 2006 Dec 22;580(30):6903-8. Epub 2006 Nov 30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17157298 17157298]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Blanco, F J.]]
[[Category: Blanco FJ]]
[[Category: Garcia, P.]]
[[Category: Garcia P]]
[[Category: Lopez-Hernandez, E.]]
[[Category: Lopez-Hernandez E]]
[[Category: Padro, D.]]
[[Category: Padro D]]
[[Category: Palacios, A.]]
[[Category: Palacios A]]
[[Category: Acetylation]]
[[Category: Alternative splicing]]
[[Category: Anti-oncogene]]
[[Category: Cell cycle]]
[[Category: Coiled coil]]
[[Category: Gene regulation]]
[[Category: Metal-binding]]
[[Category: Nucleus]]
[[Category: Phd]]
[[Category: Zinc]]
[[Category: Zinc-finger]]
[[Category: Zn]]
 
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