View source for 3zpv


==Crystal structure of Drosophila Pygo PHD finger in complex with Legless HD1 domain==
<StructureSection load='3zpv' size='340' side='right'caption='[[3zpv]], [[Resolution|resolution]] 2.68&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3zpv]] is a 36 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZPV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZPV FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.68&#8491;</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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3zpv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zpv OCA], [https://pdbe.org/3zpv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zpv RCSB], [https://www.ebi.ac.uk/pdbsum/3zpv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zpv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PYGO_DROME PYGO_DROME] Involved in signal transduction through the Wnt pathway.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Pygo proteins promote Armadillo- and beta-catenin-dependent transcription, by relieving Groucho-dependent repression of Wnt targets. Their PHD fingers bind histone H3 tail methylated at lysine 4, and to the HD1 domain of their Legless/BCL9 cofactors, linking Pygo to Armadillo/beta-catenin. Intriguingly, fly Pygo orthologs exhibit a tryptophan &gt; phenylalanine substitution in their histone pocket-divider which reduces their affinity for histones. Here, we use X-ray crystallography and NMR, to discover a conspicuous groove bordering this phenylalanine in the Drosophila PHD-HD1 complex-a semi-aromatic cage recognizing asymmetrically methylated arginine 2 (R2me2a), a chromatin mark of silenced genes. Our structural model of the ternary complex reveals a distinct mode of dimethylarginine recognition, involving a polar interaction between R2me2a and its groove, the structural integrity of which is crucial for normal tissue patterning. Notably, humanized fly Pygo derepresses Notch targets, implying an inherent Notch-related function of classical Pygo orthologs, disabled in fly Pygo, which thus appears dedicated to Wnt signaling.

Evolutionary Adaptation of the Fly Pygo PHD Finger toward Recognizing Histone H3 Tail Methylated at Arginine 2.,Miller TC, Mieszczanek J, Sanchez-Barrena MJ, Rutherford TJ, Fiedler M, Bienz M Structure. 2013 Oct 30. pii: S0969-2126(13)00364-X. doi:, 10.1016/j.str.2013.09.013. PMID:24183574<ref>PMID:24183574</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3zpv" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Drosophila melanogaster]]
[[Category: Large Structures]]
[[Category: Bienz M]]
[[Category: Fiedler M]]
[[Category: Mieszczanek J]]
[[Category: Miller TCR]]
[[Category: Rutherford TJ]]
[[Category: Sanchez-Barrena MJ]]