5b64: Difference between revisions

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 ==A novel binding mode of MAGUK GK domain revealed by DLG GK domain in complex with KIF13B MBS domain==
-<StructureSection load='5b64' size='340' side='right' caption='[[5b64]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
+<StructureSection load='5b64' size='340' side='right'caption='[[5b64]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5b64]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B64 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5B64 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5b64]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Rattus Rattus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B64 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5B64 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5b64 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b64 OCA], [http://pdbe.org/5b64 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5b64 RCSB], [http://www.ebi.ac.uk/pdbsum/5b64 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5b64 ProSAT]</span></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=SO4:SULFATE+ION'>SO4</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=5b64 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b64 OCA], [https://pdbe.org/5b64 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5b64 RCSB], [https://www.ebi.ac.uk/pdbsum/5b64 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5b64 ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[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>
-The membrane-associated guanylate kinase (MAGUK) scaffold proteins share a signature guanylate kinase (GK) domain. Despite their diverse functional roles in cell polarity control and synaptic signaling, the currently known mode of action of MAGUK GK is via its binding to phosphorylated short peptides from target proteins. Here, we discover that the GK domain of DLG MAGUK binds to an unphosphorylated and autonomously folded domain within the stalk region (MAGUK binding stalk [MBS] domain) of a kinesin motor KIF13B with high specificity and affinity. The structure of DLG4 GK in complex with KIF13B MBS reveals the molecular mechanism governing this atypical GK/target recognition mode and provides insights into DLG/KIF13B complex-mediated regulation of diverse cellular processes such as asymmetric cell division. We further show that binding to non-phosphorylated targets is another general property of MAGUK GKs, thus expanding the mechanisms of action of the MAGUK family proteins.
-An Atypical MAGUK GK Target Recognition Mode Revealed by the Interaction between DLG and KIF13B.,Zhu J, Shang Y, Xia Y, Zhang R, Zhang M Structure. 2016 Sep 15. pii: S0969-2126(16)30241-6. doi:, 10.1016/j.str.2016.08.008. PMID:27642159<ref>PMID:27642159</ref>
+==See Also==
+*[[Kinesin 3D Structures|Kinesin 3D Structures]]
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 5b64" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Shang, Y]]
+[[Category: Large Structures]]
-[[Category: Zhang, M]]
+[[Category: Mus musculus]]
-[[Category: Zhu, J]]
+[[Category: Rattus]]
-[[Category: Gk]]
+[[Category: Shang Y]]
-[[Category: Kif13b]]
+[[Category: Zhang M]]
-[[Category: Kinesin]]
+[[Category: Zhu J]]
-[[Category: Maguk]]
-[[Category: Mb]]
-[[Category: Motor]]
-[[Category: Peptide binding protein]]