4rp3

<StructureSection load='4rp3' size='340' side='right'caption='[[4rp3]], [[Resolution|resolution]] 1.36&Aring;' scene=''>

<table><tr><td colspan='2'>[[4rp3]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RP3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RP3 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</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=4rp3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rp3 OCA], [https://pdbe.org/4rp3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rp3 RCSB], [https://www.ebi.ac.uk/pdbsum/4rp3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rp3 ProSAT]</span></td></tr>

== Function ==

[[https://www.uniprot.org/uniprot/DLG1_DROME DLG1_DROME]] During embryonic development, some isoforms are essential for proper neuronal differentiation and organization. Required for cell polarity; maintenance of apicobasal polarity. Plays a critical role at septate junctions in cellular growth control during larval development. The presence of a guanylate kinase domain suggests involvement in cellular adhesion as well as signal transduction to control cellular proliferation.<ref>PMID:10884224</ref> <ref>PMID:12657668</ref> <ref>PMID:1651169</ref>

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== Publication Abstract from PubMed ==

Disc large 1 (Dlg1) proteins, members of the MAGUK protein family, are linked to cell polarity via their participation in multiprotein assemblies. At their N-termini, Dlg1 proteins contain a L27 domain. Typically, the L27 domains participate in the formation of obligate hetero-oligomers with the L27 domains from their cognate partners. Among the MAGUKs, Dlg1 proteins exist as homo-oligomers, and the oligomerization is solely dependent on the L27 domain. Here we provide biochemical and structural evidence of homodimerization via the L27 domain of Dlg1 from Drosophila melanogaster. The structure reveals that the core of the dimer is formed by a distinctive six-helix assembly, involving all three conserved helices from each subunit (monomer). The homodimer interface is extended by the C-terminal tail of the L27 domain of Dlg1, which forms a two-stranded antiparallel beta-sheet. The structure reconciles and provides a structural context for a large body of available mutational data. From our analyses, we conclude that the observed L27 homodimerization is most likely a feature unique to the Dlg1 orthologs within the MAGUK family.

Structures of the L27 Domain of Disc Large Homologue 1 Protein Illustrate a Self-Assembly Module.,Ghosh A, Ramagopal UA, Bonanno JB, Brenowitz M, Almo SC Biochemistry. 2018 Feb 27;57(8):1293-1305. doi: 10.1021/acs.biochem.7b01074. Epub, 2018 Feb 7. PMID:29261291<ref>PMID:29261291</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 4rp3" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Almo, S C]]

[[Category: Ghosh, A]]

[[Category: Structural genomic]]

[[Category: Ramagopal, U]]

[[Category: Scaffolding]]