View source for 7yki


==Crystal structure of MAGI2 PDZ0-GK domain in complex with phospho-SAPAP1 GBR3 peptide==
<StructureSection load='7yki' size='340' side='right'caption='[[7yki]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7yki]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7YKI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7YKI 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&#8491;</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>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</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=7yki FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7yki OCA], [https://pdbe.org/7yki PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7yki RCSB], [https://www.ebi.ac.uk/pdbsum/7yki PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7yki ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Dynamic signal transduction requires the rapid assembly and disassembly of signaling complexes, often mediated by phosphoprotein binding modules. The guanylate kinase-like (GK) domain of the membrane-associated guanylate kinases (MAGUKs) is such a module orchestrating signaling at cellular junctions. The MAGI subfamily of MAGUKs contains a truncated GK domain with unknown structure and function, although they participate in diverse physiological and pathological processes. Here, we demonstrate that the truncated GK domain of MAGI2 interacts with its adjacent PDZ0 domain to form a structural supramodule capable of recognizing phosphoproteins. A conserved phosphorylation-dependent binding motif for PDZ0-GK is delineated, which leads to identification of a set of previously unknown binding partners. We explore the structure and function of the MAGI2-target complex with an inhibitory peptide derived from the consensus motif. Our work reveals an action mechanism of the cryptic MAGI GKs and broadens our understanding of the target recognition rules of phosphoprotein binding modules.

Phosphorylation-dependent recognition of diverse protein targets by the cryptic GK domain of MAGI MAGUKs.,Zhang M, Cao A, Lin L, Chen Y, Shang Y, Wang C, Zhang M, Zhu J Sci Adv. 2023 May 10;9(19):eadf3295. doi: 10.1126/sciadv.adf3295. Epub 2023 May , 10. PMID:37163606<ref>PMID:37163606</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7yki" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Lin L]]
[[Category: Zhang M]]
[[Category: Zhu J]]