2vnf

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (15:26, 13 December 2023) (edit) (undo)
 
(9 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:2vnf.png|left|200px]]
 
-
<!--
+
==MOLECULAR BASIS OF HISTONE H3K4ME3 RECOGNITION BY ING4==
-
The line below this paragraph, containing "STRUCTURE_2vnf", creates the "Structure Box" on the page.
+
<StructureSection load='2vnf' size='340' side='right'caption='[[2vnf]], [[Resolution|resolution]] 1.76&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'>[[2vnf]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VNF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VNF 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">X-ray diffraction, [[Resolution|Resolution]] 1.76&#8491;</td></tr>
-
-->
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</scene>, <scene name='pdbligand=DTU:(2R,3S)-1,4-DIMERCAPTOBUTANE-2,3-DIOL'>DTU</scene>, <scene name='pdbligand=M3L:N-TRIMETHYLLYSINE'>M3L</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-
{{STRUCTURE_2vnf| PDB=2vnf | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2vnf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vnf OCA], [https://pdbe.org/2vnf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vnf RCSB], [https://www.ebi.ac.uk/pdbsum/2vnf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vnf 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/vn/2vnf_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=2vnf ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The inhibitors of growth (ING) family of tumor suppressors consists of five homologous proteins involved in chromatin remodeling. They form part of different acetylation and deacetylation complexes and are thought to direct them to specific regions of the chromatin, through the recognition of H3K4me3 (trimethylated K4 in the histone 3 tail) by their conserved plant homeodomain (PHD). We have determined the crystal structure of ING4-PHD bound to H3K4me3, which reveals a tight complex stabilized by numerous interactions. NMR shows that there is a reduction in the backbone mobility on the regions of the PHD that participate in the peptide binding, and binding affinities differ depending on histone tail lengths Thermodynamic analysis reveals that the discrimination in favor of methylated lysine is entropy-driven, contrary to what has been described for chromodomains. The molecular basis of H3K4me3 recognition by ING4 differs from that of ING2, which is consistent with their different affinities for methylated histone tails. These differences suggest a distinct role in transcriptional regulation for these two ING family members because of the antagonistic effect of the complexes that they recruit onto chromatin. Our results illustrate the versatility of PHD fingers as readers of the histone code.
-
===MOLECULAR BASIS OF HISTONE H3K4ME3 RECOGNITION BY ING4===
+
Molecular basis of histone H3K4me3 recognition by ING4.,Palacios A, Munoz IG, Pantoja-Uceda D, Marcaida MJ, Torres D, Martin-Garcia JM, Luque I, Montoya G, Blanco FJ J Biol Chem. 2008 Jun 6;283(23):15956-64. Epub 2008 Apr 1. PMID:18381289<ref>PMID:18381289</ref>
-
 
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
<!--
+
</div>
-
The line below this paragraph, {{ABSTRACT_PUBMED_18381289}}, adds the Publication Abstract to the page
+
<div class="pdbe-citations 2vnf" style="background-color:#fffaf0;"></div>
-
(as it appears on PubMed at http://www.pubmed.gov), where 18381289 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_18381289}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
-
2VNF is a 4 chains 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=2VNF OCA].
+
-
 
+
-
==Reference==
+
-
<ref group="xtra">PMID:18381289</ref><references group="xtra"/>
+
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Blanco, F J.]]
+
[[Category: Large Structures]]
-
[[Category: Luque, I.]]
+
[[Category: Blanco FJ]]
-
[[Category: Marcaida, M J.]]
+
[[Category: Luque I]]
-
[[Category: Martin-Garcia, J M.]]
+
[[Category: Marcaida MJ]]
-
[[Category: Montoya, G.]]
+
[[Category: Martin-Garcia JM]]
-
[[Category: Munoz, I G.]]
+
[[Category: Montoya G]]
-
[[Category: Palacios, A.]]
+
[[Category: Munoz IG]]
-
[[Category: Pantoja-Uceda, D.]]
+
[[Category: Palacios A]]
-
[[Category: Torres, D.]]
+
[[Category: Pantoja-Uceda D]]
-
[[Category: Acetylation]]
+
[[Category: Torres D]]
-
[[Category: Alternative splicing]]
+
-
[[Category: Anti-oncogene]]
+
-
[[Category: Cell cycle]]
+
-
[[Category: Coiled c nucleus]]
+
-
[[Category: Histone 3]]
+
-
[[Category: Ing4]]
+
-
[[Category: Phd finger]]
+
-
[[Category: Zinc]]
+
-
[[Category: Zinc-finger]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 07:41:41 2009''
+

Current revision

MOLECULAR BASIS OF HISTONE H3K4ME3 RECOGNITION BY ING4

PDB ID 2vnf

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2vnf"
Personal tools