View source for 3wp0


==Crystal structure of Dlg GK in complex with a phosphor-Lgl2 peptide==
<StructureSection load='3wp0' size='340' side='right'caption='[[3wp0]], [[Resolution|resolution]] 2.04&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3wp0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WP0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WP0 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3wp1|3wp1]]</div></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Dlg4, Dlgh4, Psd95 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</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=3wp0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wp0 OCA], [https://pdbe.org/3wp0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wp0 RCSB], [https://www.ebi.ac.uk/pdbsum/3wp0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wp0 ProSAT]</span></td></tr>
</table>
== Function ==
[[https://www.uniprot.org/uniprot/DLG4_RAT DLG4_RAT]] Interacts with the cytoplasmic tail of NMDA receptor subunits and shaker-type potassium channels. Required for synaptic plasticity associated with NMDA receptor signaling. Overexpression or depletion of DLG4 changes the ratio of excitatory to inhibitory synapses in hippocampal neurons. May reduce the amplitude of ASIC3 acid-evoked currents by retaining the channel intracellularly. May regulate the intracellular trafficking of ADR1B.<ref>PMID:15317815</ref> <ref>PMID:15358863</ref>  [[https://www.uniprot.org/uniprot/L2GL2_HUMAN L2GL2_HUMAN]] Part of a complex with GPSM2/LGN, PRKCI/aPKC and PARD6B/Par-6, which may ensure the correct organization and orientation of bipolar spindles for normal cell division. This complex plays roles in the initial phase of the establishment of epithelial cell polarity.<ref>PMID:15632202</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The tumor suppressors Discs Large (Dlg), Lethal giant larvae (Lgl) and Scribble are essential for the establishment and maintenance of epithelial cell polarity in metazoan. Dlg, Lgl and Scribble are known to interact strongly with each other genetically and form the evolutionarily conserved Scribble complex. Despite more than a decade of extensive research, it has not been demonstrated whether Dlg, Lgl and Scribble physically interact with each other. Here, we show that Dlg directly interacts with Lgl in a phosphorylation-dependent manner. Phosphorylation of any one of the three conserved Ser residues situated in the central linker region of Lgl is sufficient for its binding to the Dlg guanylate kinase (GK) domain. The crystal structures of the Dlg4 GK domain in complex with two phosphor-Lgl2 peptides reveal the molecular mechanism underlying the specific and phosphorylation-dependent Dlg/Lgl complex formation. In addition to providing a mechanistic basis underlying the regulated formation of the Scribble complex, the structure of the Dlg/Lgl complex may also serve as a starting point for designing specific Dlg inhibitors for targeting the Scribble complex formation.Cell Research advance online publication 11 February 2014; doi:10.1038/cr.2014.16.

Phosphorylation-dependent interaction between tumor suppressors Dlg and Lgl.,Zhu J, Shang Y, Wan Q, Xia Y, Chen J, Du Q, Zhang M Cell Res. 2014 Feb 11. doi: 10.1038/cr.2014.16. PMID:24513855<ref>PMID:24513855</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3wp0" style="background-color:#fffaf0;"></div>

==See Also==
*[[Postsynaptic density protein 3D structures|Postsynaptic density protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Buffalo rat]]
[[Category: Large Structures]]
[[Category: Chen, J]]
[[Category: Du, Q]]
[[Category: Shang, Y]]
[[Category: Wan, Q]]
[[Category: Xia, Y]]
[[Category: Zhang, M]]
[[Category: Zhu, J]]
[[Category: Cell polarity]]
[[Category: Maguk]]
[[Category: Peptide binding protein]]
[[Category: Phosphorylation]]
[[Category: Phosphorylation dependent]]
[[Category: Tumor suppressor]]