2k1j: Difference between revisions

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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=''>
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'>[[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>
or leave the SCENE parameter empty for the default display.
</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>
'''Plan homeodomain finger of tumour supressor ING4'''
== 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 ==
==Overview==
[[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].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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.
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.


==About this Structure==
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>
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 crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K1J OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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]
</div>
<div class="pdbe-citations 2k1j" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[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]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 16 23:02:55 2008''

Latest revision as of 22:08, 29 May 2024

Plan homeodomain finger of tumour supressor ING4Plan homeodomain finger of tumour supressor ING4

Structural highlights

2k1j is a 1 chain structure with sequence from Homo sapiens. This structure supersedes the now removed PDB entry 2jmq. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).[1] [2] [3] [4] [5] [6]

Evolutionary Conservation

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

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.

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[7]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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. ↑ Zhang X, Xu LS, Wang ZQ, Wang KS, Li N, Cheng ZH, Huang SZ, Wei DZ, Han ZG. ING4 induces G2/M cell cycle arrest and enhances the chemosensitivity to DNA-damage agents in HepG2 cells. FEBS Lett. 2004 Jul 16;570(1-3):7-12. PMID:15251430 doi:http://dx.doi.org/10.1016/j.febslet.2004.06.010
  3. ↑ Garkavtsev I, Kozin SV, Chernova O, Xu L, Winkler F, Brown E, Barnett GH, Jain RK. The candidate tumour suppressor protein ING4 regulates brain tumour growth and angiogenesis. Nature. 2004 Mar 18;428(6980):328-32. PMID:15029197 doi:http://dx.doi.org/10.1038/nature02329
  4. ↑ Kim S, Chin K, Gray JW, Bishop JM. A screen for genes that suppress loss of contact inhibition: identification of ING4 as a candidate tumor suppressor gene in human cancer. Proc Natl Acad Sci U S A. 2004 Nov 16;101(46):16251-6. Epub 2004 Nov 4. PMID:15528276 doi:http://dx.doi.org/10.1073/pnas.0407158101
  5. ↑ Ozer A, Wu LC, Bruick RK. The candidate tumor suppressor ING4 represses activation of the hypoxia inducible factor (HIF). Proc Natl Acad Sci U S A. 2005 May 24;102(21):7481-6. Epub 2005 May 16. PMID:15897452 doi:0502716102
  6. ↑ 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
  7. ↑ Palacios A, Garcia P, Padro D, Lopez-Hernandez E, Martin I, Blanco FJ. Solution structure and NMR characterization of the binding to methylated histone tails of the plant homeodomain finger of the tumour suppressor ING4. FEBS Lett. 2006 Dec 22;580(30):6903-8. Epub 2006 Nov 30. PMID:17157298 doi:10.1016/j.febslet.2006.11.055
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