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==Crystal Structure of the 3rd PDZ domain of the human Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 3 (MAGI3)== | |||
<StructureSection load='3soe' size='340' side='right'caption='[[3soe]], [[Resolution|resolution]] 1.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3soe]] is a 1 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=3SOE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SOE 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]] 1.6Å</td></tr> | |||
== | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> | ||
[[3soe]] is a 1 chain structure | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3soe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3soe OCA], [https://pdbe.org/3soe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3soe RCSB], [https://www.ebi.ac.uk/pdbsum/3soe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3soe ProSAT]</span></td></tr> | ||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/MAGI3_HUMAN MAGI3_HUMAN] Acts as a scaffolding protein at cell-cell junctions, thereby regulating various cellular and signaling processes. Cooperates with PTEN to modulate the kinase activity of AKT1. Its interaction with PTPRB and tyrosine phosphorylated proteins suggests that it may link receptor tyrosine phosphatase with its substrates at the plasma membrane. In polarized epithelial cells, involved in efficient trafficking of TGFA to the cell surface. Regulates the ability of LPAR2 to activate ERK and RhoA pathways. Regulates the JNK signaling cascade via its interaction with FZD4 and VANGL2.<ref>PMID:10748157</ref> | |||
==See Also== | ==See Also== | ||
*[[Guanylate kinase|Guanylate kinase]] | *[[Guanylate kinase 3D structures|Guanylate kinase 3D structures]] | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Arrowsmith CH]] | ||
[[Category: | [[Category: Bountra C]] | ||
[[Category: Edwards | [[Category: Edwards A]] | ||
[[Category: Filippakopoulos | [[Category: Filippakopoulos P]] | ||
[[Category: Ivarsson | [[Category: Ivarsson Y]] | ||
[[Category: Knapp | [[Category: Knapp S]] | ||
[[Category: Picaud | [[Category: Picaud S]] | ||
[[Category: Vollmar M]] | |||
[[Category: Vollmar | [[Category: Weigelt J]] | ||
[[Category: Weigelt | [[Category: Zimmermann P]] | ||
[[Category: Zimmermann | [[Category: Von Delft F]] | ||
[[Category: | |||
Latest revision as of 16:03, 14 March 2024
Crystal Structure of the 3rd PDZ domain of the human Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 3 (MAGI3)Crystal Structure of the 3rd PDZ domain of the human Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 3 (MAGI3)
Structural highlights
FunctionMAGI3_HUMAN Acts as a scaffolding protein at cell-cell junctions, thereby regulating various cellular and signaling processes. Cooperates with PTEN to modulate the kinase activity of AKT1. Its interaction with PTPRB and tyrosine phosphorylated proteins suggests that it may link receptor tyrosine phosphatase with its substrates at the plasma membrane. In polarized epithelial cells, involved in efficient trafficking of TGFA to the cell surface. Regulates the ability of LPAR2 to activate ERK and RhoA pathways. Regulates the JNK signaling cascade via its interaction with FZD4 and VANGL2.[1] See AlsoReferences
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